MCPymol — talk to PyMOL

MCPymol is a Model Context Protocol server that lets you drive PyMOL with natural language. Load structures, set up analytical views, measure things, and explore proteins by talking to Claude or Gemini. The image above was made by typing "show me a nucleosome" into Claude Code. That was the whole prompt.

PyMOL is great, but its syntax is famously obscure — and despite the name, it isn't quite Python. MCPymol is for people who'd rather just look at structures.

What you get

• A vocabulary the LLM understands. Tools like fetch_structure, ligand_view, interface_view, mutation_view, conservation_view do high-level setup in one call: pick the biological assembly, hide solvent, color sensibly, label the right residues, draw the right H-bonds.

• Renders the model can see. render ray-traces and hands the image straight back, so the assistant can look at what it made and fix it — rather than writing a PNG it has no way to inspect.

• 87 PyMOL primitives exposed as individual tools (show, hide, color, select, distance, align, spectrum, …) so the model can compose finer motions when the high-level tools don't quite fit. 121 tools in total, every parameter documented in the tool schema. When even that runs out, execute_pymol_command passes a raw PyMOL command straight through.

• Predicted structures. A UniProt accession fetches from AlphaFold DB and colors by pLDDT confidence in the official palette — via fetch_structure or fetch_alphafold directly.

• Scene introspection. list_objects, list_chains, list_ligands and structure_info let the model check what's actually loaded before guessing, count_atoms catches a selection that matches nothing — otherwise invisible until the render comes out blank — and atom_properties reaches occupancy and altlocs that no per-residue view can show.

• Your own files too. load_structure opens a local PDB/mmCIF — a model you built, a docking pose, an MD frame — through the same prep and styling as a fetched entry.

• Smart structure prep. Fetching a PDB code grabs the biological assembly when one exists, then runs a BFS heuristic over chain–chain contacts (multimer_cutoff, default 8 Å) so sprawling functional multimers like the CRP pentamer or ferritin cage stay whole while crystallographic copies get dropped. Waters and crystallization additives are hidden automatically.

• Two-process bridge. PyMOL's GUI has its own Python; MCPymol works by running a tiny TCP listener inside PyMOL plus a separate FastMCP server outside it.

Related MCP server: PubMed MCP Server

How it talks

┌──────────────┐   MCP / stdio    ┌────────────────┐  JSON over TCP  ┌──────────────┐
│ Claude /     │ ───────────────▶ │ mcpymol server │ ◀────:9876────▶ │ PyMOL GUI    │
│ Gemini CLI   │                  │   (FastMCP)    │                 │  (plugin.py) │
└──────────────┘                  └────────────────┘                 └──────────────┘

The plugin half runs inside PyMOL and dispatches to pymol.cmd. The bridge half is what the MCP client launches. They talk over a local TCP socket because PyMOL's GUI ships its own Python interpreter, which cannot import the packages the MCP server needs — so the two halves cannot live in one process.

Both halves must run on the same machine: several tools hand files between them through the filesystem.

Try it

"Fetch ubiquitin (1ubq) and show it as a cartoon, then show me the render." "Color the alpha helices red and the beta sheets blue." "What ligands are in 1HSG?" "Show the binding pocket around MK1 in 1HSG." "Highlight mutations E6V, K16E, and V67F in hemoglobin (4HHB)." "Run a Poisson-Boltzmann electrostatics calculation on 1LYZ." "Get the AlphaFold model for P69905 and tell me how confident it is." "Superpose 1AKE onto 4AKE and show me where adenylate kinase moves." "Make me a turntable animation of the nucleosome."

Tip: if the model isn't sure what's loaded, ask it to list the objects — it'll call list_objects and ground itself before guessing names.

What can I ask?

Organised by the question, not the tool.

The pattern that works best: report first, then draw. contact_report tells you Asp30 makes a salt bridge at 2.7 Å; ligand_view then shows you where it sits. Asking only for the picture gets you a picture you have to interpret yourself.

Requirements

• PyMOL — the open-source build is what this is developed against (brew install pymol on macOS, apt-get install pymol on Debian/Ubuntu). The Schrödinger incentive build works too. MCPymol drives a PyMOL you already have; it does not install or bundle one.

• Python 3.10+ for the bridge. This is separate from the Python inside PyMOL, which MCPymol never imports into.

• An MCP client — Claude Code, Claude Desktop, or Gemini CLI.

Optional, per feature:

Installation

There are two halves to wire up: the native plugin (runs inside PyMOL) and the MCP bridge (runs outside, and is what your AI assistant launches). Both come from the same package.

1. Install MCPymol

uv tool install mcpymol

pipx install mcpymol works the same way. There is no need to clone the repository unless you intend to work on MCPymol itself.

Check it landed somewhere your shell can see:

which mcpymol      # if this prints nothing, run: uv tool update-shell

Note the full path it prints — you will want it in step 3. uv and pipx install into ~/.local/bin, which is not on everyone's PATH, and an MCP client started by the OS rather than from your shell does not inherit your PATH at all. Wiring the assistant to a bare mcpymol when it is not on PATH fails at launch with spawn mcpymol ENOENT, not at install time.

Why not uvx mcpymol? uvx runs the bridge perfectly well, but it is the wrong tool for step 2: it unpacks the package into ~/.cache/uv, and the plugin has to be loaded by absolute path, so the line written into your PyMOL startup file would point into a cache that uv cache clean reclaims. uv tool install puts it somewhere permanent — and lets both halves come from one installation, so the bridge and the plugin cannot drift apart.

2. Start the native plugin

The plugin runs inside PyMOL, which has its own Python interpreter — it cannot import the installed package, so it is loaded from a file path. Let MCPymol find that path for you:

mcpymol --install-plugin

That adds a small managed block to ~/.pymolrc.py, so PyMOL loads the plugin on every launch. Restart PyMOL and you should see:

MCPymol Native Plugin listening on 127.0.0.1:9876

Re-run it after upgrading MCPymol — the block embeds a path into one installation and is rewritten, not duplicated. mcpymol --uninstall-plugin removes it and leaves the rest of your .pymolrc.py alone.

If you would rather wire it up yourself, mcpymol --plugin-path prints the path, and you can run it from the PyMOL command line or add your own line to ~/.pymolrc.py.

Changing the port. Set MCPYMOL_PORT before launching both PyMOL and the bridge — see Configuration.

3. Register the bridge with your AI assistant

Pick one. Use the full path from which mcpymol — it is the same installation the plugin came from, and a bare mcpymol only works if that directory is on the PATH of whatever launches the client.

Claude Code CLI

claude mcp add mcpymol -- "$(which mcpymol)"

Start a new Claude Code session.

Claude Desktop

Add to claude_desktop_config.json:

{
  "mcpServers": {
    "mcpymol": {
      "command": "/absolute/path/to/mcpymol"
    }
  }
}

The absolute path is not optional here: Claude Desktop is launched by the OS rather than from your shell, so it never inherits your PATH. Restart Claude Desktop afterwards.

Gemini CLI

gemini mcp add mcpymol "$(which mcpymol)"
gemini mcp refresh

Without installing — uvx

To run the bridge without installing anything, point your assistant at uvx mcpymol:

claude mcp add mcpymol -- uvx mcpymol

You still need the plugin, and step 2's command is not available to you — nothing was installed. Run it through uvx instead:

uvx mcpymol --install-plugin

That writes a path into ~/.cache/uv (see the note in step 1), so uv cache clean or a uvx upgrade will break it and you will have to re-run it. uvx also resolves the newest release on each launch, so the bridge can drift ahead of the plugin. This path trades a permanent install for maintenance; if that sounds worse than installing, install.

Restricted environments — no uv

If uv is blocked by your org's security policy, use a standard venv. On Linux you may need sudo apt-get install python3-venv pymol first.

python3 -m venv ~/.venvs/mcpymol
~/.venvs/mcpymol/bin/pip install --upgrade pip
~/.venvs/mcpymol/bin/pip install mcpymol
~/.venvs/mcpymol/bin/mcpymol --install-plugin

# Point the assistant directly at the venv binary
claude mcp add mcpymol ~/.venvs/mcpymol/bin/mcpymol
# or
gemini mcp add mcpymol ~/.venvs/mcpymol/bin/mcpymol

If your network blocks PyPI, install from your internal mirror with pip install --index-url ....

Upgrading

Upgrade the way you installed — uv tool upgrade mcpymol, pipx upgrade mcpymol, or <venv>/bin/pip install --upgrade mcpymol. Then restart PyMOL and reconnect the MCP server in your client (/mcp in Claude Code).

Both halves have to move together, and neither moves on its own. The plugin is loaded into PyMOL's memory at startup, and the bridge is a process your MCP client launched — upgrading the package on disk changes neither until each is restarted. PyMOL will happily keep running the plugin it loaded days ago against a freshly upgraded bridge.

You do not normally need to re-run --install-plugin: uv tool, pipx and a venv all upgrade the package in place, so the path in ~/.pymolrc.py still points at the right file. Re-run it if you move the installation — switching install method, rebuilding the venv, or using the uvx path, whose cache directory does change.

A mismatched pair fails in a way that reads like a bug in a tool rather than a stale process: calls that should work report unknown actions, or a tool fixed in the release you just installed keeps misbehaving.

Working on MCPymol itself

For development, clone the repo and run from the checkout — this is the only path that needs a clone:

git clone https://github.com/chemrich/MCPymol.git
cd MCPymol
uv sync
uv run mcpymol --install-plugin
claude mcp add mcpymol -- uv --directory /absolute/path/to/MCPymol run mcpymol

See CONTRIBUTING.md.

Configuration

Everything is optional; the defaults are what the tools are tuned for. Set them before launching PyMOL and the bridge.

MCPYMOL_PORT=9867 open -a PyMOL       # macOS
MCPYMOL_PORT=9867 mcpymol             # bridge

Troubleshooting

Tests

uv run pytest

555 tests run by default. They mock the socket layer and PyMOL's cmd module, so they need neither PyMOL nor a network, and cover the socket payloads, the bridge framing, the conservation pipeline (A3M parsing, Shannon entropy, MMseqs2 mocking, MSA→B-factor mapping), the mesh-repair paths, and every view. tests/test_bridge_roundtrip.py additionally runs the real bridge against the real plugin listener over TCP on an ephemeral port, so the wire format is checked against itself rather than against a mock.

The two opt-in suites

A further 122 tests are deselected by default, because they need things CI does not have. Both are worth running before a release tag:

uv run pytest -m live      # needs a running PyMOL with the plugin loaded
uv run pytest -m network   # hits real external APIs

-m live clears the PyMOL session it connects to. It drives your actual PyMOL. Don't run it against a session you care about.

-m live exists because a mocked suite asserts the payload we send, which can never tell you whether PyMOL will accept it — and that gap is where every wiring bug has lived: tools calling cmd functions that don't exist, arguments bound in the wrong order, renders that come back blank. It calls every registered tool once and asserts only that each is wired (the action resolves, the arguments bind), not that it succeeds, since many tools error honestly without the right context. New tools are swept automatically. It skips cleanly when no PyMOL is listening, and detects a wedged session rather than reporting a hundred confusing failures.

Treat a green default run as necessary, not sufficient.

Layout

mcpymol/server.py is the entry point and re-exports everything, so from mcpymol.server import ligand_view still works.

The view library

These are the high-level visualization tools. Each does its own setup — coloring, transparency, H-bonds, labels — in one prompt.

ligand_view — binding site

Pocket residues (within 5 Å of the ligand) as element-colored sticks with CA labels, ligand as yellow sticks, H-bonds as yellow dashes, protein as a translucent cartoon.

Show me the ATP binding site in 1ATP

interface_view — protein–protein interface

Chain A marine, chain B salmon. Interface residues (within 4 Å of the partner) as solid surface patches with sidechain sticks and CA labels. Cross-chain H-bonds as yellow dashes.

Show the interface between chain A and chain D in 1BRS

putty_view — B-factor flexibility

Tube radius and color scale with B-factor: blue/thin = rigid, red/thick = flexible. A 70%-transparent surface adds shape context.

Show the B-factor flexibility of 1UBQ as a putty view

bfactor_view — B-factor flexibility, plain cartoon

The same color story as putty_view (blue → red on B-factor) but on a plain cartoon. Cheaper, cleaner in figures where you don't want the putty distortion.

Color 1UBQ by B-factor

hydrophobic_surface_view — surface chemistry

Surface colored by amino-acid chemistry: orange = hydrophobic, white = polar, sky blue = positive, salmon = negative. Useful for spotting hydrophobic patches, membrane belts, and charge complementarity.

Show the hydrophobic surface of 1TCA

electrostatic_view — approximate electrostatics

Red→white→blue surface coloring driven by per-residue pKa-weighted partial charges. Two modes: atomic (charges on the actual charge-center atoms — localized, natural falloff) and residue (uniform across charged residues — saturated patches).

Show the electrostatic surface of 1LYZ

poisson_boltzmann_view — true PB electrostatics

Full Poisson-Boltzmann potential via APBS and PDB2PQR, mapped onto the surface at ±20 kT/e. Physically correct, accounts for solvent screening and ionic strength.

Prerequisites (must be on PATH):

brew install brewsci/bio/apbs
pip install pdb2pqr

Run a Poisson-Boltzmann electrostatics calculation on 1LYZ

conservation_view — evolutionary conservation

Pipeline: extract the chain's sequence → submit to MMseqs2 (ColabFold public API by default; override with MCPYMOL_MMSEQS_URL) → parse the A3M alignment → compute per-position Shannon entropy → map onto B-factor and color via cyan_white_magenta spectrum.

Magenta = conserved, white = moderate, cyan = variable. First call takes 30 s – few minutes depending on sequence length; results are cached in memory by sequence, so re-running on the same protein (or changing only the color scale) is instant.

Color lysozyme (1LYZ) by conservation

Lysozyme against 5,507 homologues. The variable surface loops go cyan while the core and the substrate-binding cleft stay magenta — conservation tracking function, which is the whole reason to compute it.

crosslink_view — disulfides & metal coordination

CYS sidechains and disulfide bonds in yellow, metal coordination bonds in orange, the rest of the protein as a thin grey cartoon.

Show the disulfide bonds in 1CEL

pocket_view — binding pocket surface

The pocket cavity (residues within 5 Å of the ligand) as a semi-transparent surface colored by chemistry. Sticks for the pocket sidechains, yellow sticks for the ligand, cyan dashes for H-bonds.

Show the binding pocket around MK1 in 1HSG

pharmacophore_view — ligand pharmacophore features

The ligand colored by pharmacophore type: violet = aromatic ring carbon, yellow = aliphatic carbon, sky blue = N (donor/acceptor), salmon = O (acceptor), gold = S, pale green = halogen. Interacting residue sticks with CA labels, cyan dashes for H-bonds.

Show the pharmacophore features of MK1 in 1HSG

mutation_view — mutation hotspots

Grey cartoon, mutated sidechains as magenta sticks with white CA labels, neighboring residues (within 4 Å) as thin element-colored sticks for packing context. Standard A123G notation; optional chain prefix A:A123G.

Highlight mutations E6V, K16E, and V67F in hemoglobin (4HHB)

textbook_view — cel-shaded illustration

White cartoon + surface with heavy ray-trace contours. The cel-shaded look kicks in after you run ray (or ask the model to render).

Make 4HHB look like a textbook illustration

cinematic_view — fog and shadows

Depth-cueing + fog + soft shadows on a black background. Best on big assemblies — ribosomes, capsids, nucleosomes — where you want a sense of scale. Run ray for the full effect.

Give me a cinematic view of GroEL

Depth cueing needs scale to pay off — this is one GroEL ring down its seven-fold axis. On a small globular protein the effect is mostly lost.

pointillist_view — starfield surface

Replaces the surface with a dense dot cloud; ligands become bright yellow stars. More art than analysis.

plddt_view — AlphaFold confidence

Colors a predicted model by pLDDT in AlphaFold's official palette: dark blue >90 (very high), light blue 70–90 (confident), yellow 50–70 (low), orange <50 (very low). Reports the breakdown, e.g. "very high: 62%, confident: 21%, …".

pLDDT is stored in the B-factor column, which is why bfactor_view and putty_view render these models backwards — they read low B as rigid, whereas low pLDDT means the model doesn't know. plddt_view warns if the B-factors don't look like pLDDT at all.

Get the AlphaFold model for P0DTC2

Mean pLDDT 67.1 across 1273 residues — 7% very high, 49% confident, 20% low, 24% very low. The orange tails are the point: AlphaFold is telling you it does not know where they go, and no amount of rendering makes that a structure.

superposition_view — where two structures differ

Superposes mobile onto target, then colors the mobile structure by how far each residue's CA actually moved: blue = unchanged, red = most shifted. The target stays as a grey reference. Reports the RMSD, the mean and max shift, and names the worst-shifted residues.

An RMSD alone tells you a structure moved; this tells you where.

Superpose 4AKE onto 1AKE and show me where it moves

Adenylate kinase, open against closed: the core fits at 2.07 Å RMSD while residues 145–152 move up to 24 Å. That is the LID domain closing over the substrate, and it is the whole reason to colour by deviation rather than quote one number.

Both structures have to be loaded at once, and fetch_structure clears the session by default — fetch the second with replace=False. Compare single chains when the entries are multimers: superposing one dimer onto another fits the assembly rather than the fold, which reports 18.5 Å for this same pair.

Analysis — answers with numbers

The view presets draw interactions; these report them. Both matter, and they compose: run the report to get the numbers for your figure legend, run the view to make the figure.

contact_report — what touches what

Lists contacting residue pairs closest first, with the minimum heavy-atom distance, how many atoms are involved, and a classification: salt bridge, hydrogen bond, hydrophobic, polar contact, or π-stacking (parallel vs T-shaped from the interplanar angle).

contact_report("1hsg and resn MK1", "1hsg and polymer")

Criteria are heavy-atom distances — salt bridge ≤ 4.0 Å between charged sidechain tips, H-bond ≤ 3.5 Å between N/O pairs, hydrophobic ≤ 4.5 Å between C/S, ring centroids ≤ 5.5 Å — because crystal structures usually have no hydrogens. A reported hydrogen bond is therefore a donor–acceptor pair with plausible geometry, not one verified against a hydrogen position.

Ring perception needs bond orders, which a PDB dump doesn't carry, so aromatics are detected for the standard aromatic amino acids only; ligand rings show up as hydrophobic contacts rather than being mis-called as stacking.

What holds MK1 in the HIV protease pocket?

26 residue pairs in contact within 4.0 A between '1hsg and resn MK1' and '1hsg and polymer':

  B/MK1902     -- B/ASP25       2.63 A  hydrogen bond, polar contact, contact (8 atom contacts)
  B/MK1902     -- A/ASP25       2.77 A  hydrogen bond, contact (8 atom contacts)
  B/MK1902     -- B/GLY27       3.03 A  hydrogen bond, polar contact, contact (8 atom contacts)
  B/MK1902     -- B/ASP29       3.06 A  hydrogen bond, polar contact, contact (6 atom contacts)
  B/MK1902     -- A/GLY48       3.15 A  hydrophobic, contact (6 atom contacts)
  B/MK1902     -- B/VAL32       3.32 A  hydrophobic (2 atom contacts)
  ... and 20 more pairs (raise max_pairs to see).

Interaction types across all pairs: 20 hydrophobic, 14 contact, 5 hydrogen bond, 4 polar contact.

Both copies of the catalytic Asp25 — one from each chain of the protease dimer — hydrogen bond the inhibitor at 2.63 and 2.77 Å. That is the interaction the drug was designed to make, read straight off the structure. It is the same pocket the ligand_view image above shows; the picture and the numbers are two views of one question.

interface_report — how big is this interface

Buried surface area from ΔSASA (free minus bound), the per-side figure papers quote, a ranking of residues by how much surface each buries, and a breakdown by residue chemistry.

It also interprets the number: under ~400 Ų per side is usually crystal packing rather than a biological interface; over ~1000 Ų is a substantial, likely specific association. Guidance from PDB-wide surveys, not a verdict.

How big is the barnase–barstar interface in 1BRS?

Interface between chains A and D of 1brs:
  Buried surface area: 777 A^2 per side (1,553 A^2 total).
  That is a typical size for a specific but transient protein-protein interface.
  Interface residues: 22 in chain A, 19 in chain D.
  Composition by buried area: 41% charged, 32% polar, 28% hydrophobic.
  Chain A hot spots: ARG59 (154 A^2), HIS102 (107 A^2), ARG83 (78 A^2), GLU60 (69 A^2), ...
  Chain D hot spots: ASP35 (120 A^2), TYR29 (97 A^2), ASP39 (86 A^2), TRP44 (75 A^2), ...

Barnase–barstar is the textbook electrostatically-driven interface, and the numbers say so unprompted: 41% of the buried area is charged, and the hot spots it ranks — Arg59/His102 on barnase, Asp35/Asp39/Trp44 on barstar — are the residues the mutagenesis literature identifies.

structure_info and get_sequence — what am I looking at

structure_info combines what PyMOL knows (chains, counts, ligands, states, space group) with RCSB entry metadata (title, method, resolution, release date, source organism), and flags a probable AlphaFold model when the B-factor column looks like pLDDT.

1hsg — CRYSTAL STRUCTURE AT 1.9 ANGSTROMS RESOLUTION OF HUMAN IMMUNODEFICIENCY
VIRUS (HIV) II PROTEASE COMPLEXED WITH L-735,524, AN ORALLY BIOAVAILABLE
INHIBITOR OF THE HIV PROTEASES
  X-RAY DIFFRACTION, 2.00 A resolution, released 1996-04-03
  Source: Human immunodeficiency virus 1
  1,686 atoms, 198 residues, 127 waters
  Chains (2): A, B
  Ligands in '1hsg': MK1
  Space group P 21 21 2, cell 59.6 x 87.1 x 46.7 A

atom_properties reads properties that live on individual atoms rather than residues or objects — occupancy, alternate conformations, per-atom B-factor, formal charge. Nothing else reaches them: the PyMOL call that exposes them returns an object that cannot cross the bridge, so the plugin flattens it on the way out.

2 atoms in '1hsg and resi 25':

  chain  resi  resn  name  b      q
  A      25    ASP   OD1   18.42  1.00
  A      25    ASP   OD2   21.07  0.50

That 0.50 is the tool's reason to exist: a sidechain modelled in two conformations, invisible to every per-residue view.

get_sequence returns FASTA — plus the two things the sequence alone hides and that routinely cause mistakes: the numbering offset (PDB numbering rarely starts at 1, so "residue 50" in a paper and position 50 in the sequence are usually different residues) and chain breaks where loops went unmodelled.

Rendering and sessions

render — see what you made

Ray-traces the current scene and returns the image as MCP image content, so the model can actually look at it and iterate. This is the tool to use instead of ray + png, which only leave a file behind.

Defaults to 1000×750 — the image is inlined into the conversation, and base64 inflates it by a third. Above 5 MB (MCPYMOL_MAX_IMAGE_BYTES) it returns the path instead, and keeps the file there even if you did not pass a filename, so a render that took minutes is not thrown away for being too big to show.

Every render is ray-traced, and ray_trace=False does not change that: PyMOL's fast unshaded frame grab needs its GUI thread, which the plugin does not run on, so that path wrote blank images. The flag is accepted and ignored, with a note in the reply, rather than silently handing back a blank PNG. To make a render cheaper, ask for a smaller width/height. render also detects the two ways an image comes back empty — a single flat colour, or nothing written at all — and says so instead of returning a black square.

turntable — 360° animation

Writes a numbered PNG sequence spinning the camera a full turn, plus the ffmpeg command to assemble it. Defaults to 36 frames (10° apart) at 800×600.

Every frame is ray-traced, for the same reason render is — the unshaded OpenGL path silently produced blank frames over this bridge. That makes it slow: 36 frames of a large assembly can take an hour, so start with a low frames count and a small width/height before committing to a long run.

Make me a turntable animation of 1AOI

save_session / load_session — keep a scene

.pse round-trips the entire session: every object, selection, representation, color, scene and the camera. Save before experimenting with a scene that took effort to build. load_session(merge=True) adds a saved scene to the current one rather than replacing it.

🖨️ 3D Printing Export

The print_export tool turns a structure into watertight STL files ready for multi-colour 3D printing. PyMOL's open-source build can't write STL and its OBJ exporter dumps the whole visible scene as non-manifold surface soup — print_export works around all of that: it isolates each colour group, exports it, and rebuilds a single watertight, manifold solid per group. Every group stays in the same coordinate frame, so a slicer can load them as aligned multi-material parts.

This tool needs the optional print extra (trimesh, pymeshlab, scipy, scikit-image, networkx):

Install it into the same environment MCPymol is already in — a bare pip install picks whatever pip is first on your PATH, which is usually a different interpreter entirely, and leaves print_export still reporting the dependencies missing:

uv tool install 'mcpymol[print]'                   # if you used uv tool
pipx install --force 'mcpymol[print]'              # if you used pipx
~/.venvs/mcpymol/bin/pip install 'mcpymol[print]'  # if you used a venv
uv sync --extra print                              # from a checkout

Re-running over an existing install is fine — it adds the extra in place.

Export T7 RNA polymerase (1MSW) for 3D printing with the protein and the
nucleic acid as separate colours

This produces one STL per group (e.g. 1MSW_protein.stl, 1MSW_nucleic.stl). method="auto" (default) picks the cheapest path that works: compact structures (e.g. a GFP barrel) often export already-watertight, so it does a light cleanup — keeping the largest body and dropping tiny internal cavity shells — rather than Poisson, which can degrade an already-closed surface. Otherwise it falls back to Poisson, then voxel. method="poisson" forces detail-preserving reconstruction (best for bulky chains); method="voxel" is robust for thin nucleic acids and slightly thickens fragile features for printability. In your slicer, load the first STL, then add the others as parts (don't re-centre) and assign a filament per part.

print_ribbon_view — print-ready chunky ribbons

A preset that solves the classic problem of printing cartoons: PyMOL builds each β-strand and loop as a separate mesh segment, so the strand→loop junctions have no connecting geometry and slice into fragile, disconnected pieces. print_ribbon_view configures chunky β-strand arrows and a fat helix, hides the loop cartoon, and adds a continuous backbone spine (<obj>_spine, a cartoon tube that ignores secondary structure and runs unbroken through the whole chain). Exported together the voxel step fuses them into one watertight solid with no junction discontinuity — and the spine doubles as internal rebar for print rigidity. Tune spine_radius for more or less reinforcement.

print_ribbon_view(obj_name="1ema")
print_export(obj_name="1ema", groups="1ema=(1ema or 1ema_spine)",
             representation="cartoon", method="voxel", voxel_pitch=0.2)

GFP's β-barrel with the chunky arrows applied. The bulges running along each strand are the spine tube passing through — the internal rebar, visible before it gets fused into one solid on export.

Cryo-EM: occupancy, ensembles and maps

Ten tools for the things a viewer usually throws away. Every one of them exists because a render that looked fine was hiding something, so they share a rule: say what is being shown, and refuse when the picture would be meaningful-looking and wrong.

occupancy_view and altloc_view — is this atom really there

occupancy_view colours and scales by per-atom occupancy q, de-emphasising alternates at q<1 in proportion, so a half-occupied conformer looks half-there. altloc_view shows every alternate location at once, one colour per group, occupancies labelled — PyMOL shows one by default, which quietly turns a statement about heterogeneity into a single structure.

"Occupancy" names two incompatible quantities: the crystallographic q above, and the fraction of imaged particles containing a subunit. A model can be q = 1.0 everywhere while its subunit is present in half the particles. Both are true, they are different questions, and occupancy_view reports only the first — the legend says which.

occupancy_view(obj_name="1ejg")
altloc_view(obj_name="1ejg")

ensemble_spread_view and morph_states — how much do the states disagree

ensemble_spread_view computes per-residue RMS deviation across the states of a multi-model object, pushes it into the B-factor column and putty-scales it, so spread reads as tube width as well as colour. Spread is a description of how much the deposited members differ — not a calibrated uncertainty and not an error bar.

morph_states interpolates between states, and the value in it is the refusal. A morph is only meaningful when every state shares a topology; across independently reconstructed volumes it animates a correspondence nobody established, so the tool checks and declines. (cmd.morph is Incentive-only — on open-source PyMOL the check still runs and reports, and only the interpolation is unavailable.)

restore_bfactors puts back what these views overwrote.

ensemble_spread_view(obj_name="1l2y")
morph_states(obj_name="1l2y", validate_only=True)

qscore_view — per-residue model quality, already published

Colours a model by Q-score parsed straight out of its wwPDB validation report. No network, no map, no computation — the numbers exist, nothing surfaces them. Two things to expect from real data: entries deposited before the September 2023 rollout carry no Q-scores at all, and real Q-scores go negative, so the published 0–1 framing is the intended range rather than the observed one.

qscore_view(obj_name="9c0k", validation_path="9c0k_validation.xml.gz")

map_info — the number nothing displays

Reads an MRC/CCP4 header and reports the geometry, above all voxel size. Only the 1024-byte header is read: the data is never loaded, PyMOL is never touched, nothing goes over the network.

Voxel size is not stored, it is derived, and the derivation has a trap — it is cella/m (the grid sampling), not cella/n (the stored extent). Those differ on any boxed or cropped map, and dividing by n gives a wrong answer of the right order of magnitude. The nominal value is itself only expected to be accurate to ±5–15%, which at 1.2 Å is a systematic stretch of every distance in the model that looks like a slightly strained structure rather than an error. Anisotropy, cropping and axis permutation are all flagged loudly.

load_map and density_view — contouring honestly

load_map parses the header before touching PyMOL, so a malformed file fails without leaving a half-loaded object, confirms the object arrived rather than assuming it, and records provenance — which defaults to unknown and is never inferred. A measured reconstruction, a sharpened map, a network-enhanced map and a decoder output are the same isosurface once drawn, so defaulting to "measured" would assert that somebody observed a generated volume.

density_view draws an isomesh around a selection and states the contour level in both σ and absolute units. PyMOL normalises maps on load, so its levels are in σ; EMDB's author-recommended contour is an absolute map value. They are not interchangeable and the difference is not subtle — EMD-30913 publishes 0.05, which is 3.16 σ; used directly it contours noise.

load_map(path="emd_30913.map.gz", name="emd30913", provenance="measured")
density_view(map_obj="emd30913", selection="chain A", level=0.05, units="absolute")

local_resolution_view — where the map is actually good

Colours a map's isosurface by a local-resolution volume instead of by chain. A single global resolution number misrepresents almost every map: a rigid core at 2.5 Å and a flexible periphery at 5 Å live in the same volume.

Two things make this harder than it looks. The volumes must share a voxel grid — colouring one map by another samples it at the first map's coordinates, so a mismatch in extent, spacing, origin or axis order draws colour from the wrong place and renders smooth, plausible and wrong. The tool refuses and names what differs. And because PyMOL normalises on load, ramp breakpoints given in Å are converted to σ against the resolution map's own header — a different σ scale from the contour level, which comes from the density map's. Every breakpoint is reported in both units.

Local resolution is an estimate: estimators disagree with each other on the same map, and the value at a voxel depends on the window and the mask as much as on the data.

local_resolution_view(map_obj="emd30913", res_obj="emd30913_locres",
                      level=0.05, units="absolute")

Ensembles — motion, and what not to claim from it

Four tools for heterogeneity job output, and one result governs all of them. The Flatiron Institute blind challenge put 41 submissions on the same thyroglobulin data: the motions they recovered resembled both each other and the ground truth, but the simulated truth had three population modes, most submissions found two, and only three of 41 found all three. The one they missed was the middle. So: motion is recoverable, populations are not, and these tools draw the first and decline to draw the second.

load_ensemble reads a job directory — cryoDRGN, 3DVA, RECOVAR, 3DFlex, DynaMight — as ordered frames. They all write the same shape to disk: a directory of maps plus a table of latent coordinates. Frames are sorted naturally, so frame 10 does not land between 1 and 2 and silently reorder the motion. The method is identified from documented markers and never guessed; an unrecognised directory still loads, and simply stays unidentified.

latent_traverse_view contours those frames into a steppable trajectory. It refuses when the method was never identified — that is invariant I2, and the refusal is the point: cryoDRGN's latent density can bear no relation to the truth while 3DVA's frames are linear interpolations no particle occupied, so drawing them identically asserts something for one that holds only for the other. It draws no latent scatter and estimates no density, because the rendering users most want from latent space is the one the evidence says is most often wrong.

It also closes a trap specific to trajectories. PyMOL normalises every map independently on load, so contouring each frame at "1.5 σ" contours each at its own σ — and a traversal is exactly the case where density genuinely changes between frames. That is the signal, and per-frame normalisation rescales it away, leaving frames that look reassuringly alike whatever the ensemble does. So the level is held in absolute terms and converted per frame, and the spread of the resulting σ values is reported, because that spread is the change.

deformation_view is the confident one — per-residue displacement between two states, as colour and as arrows. It refuses states with differing atom counts, since atoms cannot be paired across them. Where a method estimates deformation on independent half-sets, pass that table and the arrows are coloured by the disagreement; without it, every arrow is drawn with identical confidence and they do not have identical confidence, which the report says out loud.

composition_view is occupancy in sense 2 — the fraction of imaged particles containing a part, which is a different quantity from the per-atom q that occupancy_view shows. A model can be q = 1.0 at every atom while the subunit it belongs to is present in half the particles; both are true and they answer different questions. So the fractions come from an explicit table and are never derived from q. The two tools stay separately named forever.

load_ensemble(directory="job042_cryodrgn", name="drgn", method="cryodrgn")
latent_traverse_view(ensemble_name="drgn")
deformation_view(obj_name="1l2y", arrows=True)
composition_view(obj_name="complex", table="chain A=1.0, chain B=0.38")

The name

My best friend in high school once shared an apartment with MC Chris, who voiced MC Pee Pants in Aqua Teen Hunger Force. I'm not saying that was the inspiration for the name of this project, but I'm not denying it either.

Provenance

Built on macOS using the open-source PyMOL available via Homebrew. Started with Antigravity, then Gemini Pro 3.1 until I ran out of tokens, then Claude Code (Sonnet 4.6 thinking). Tested with Claude Code and Gemini CLI. Conservation analysis uses the ColabFold public MMseqs2 API (please don't hammer it).

License

MIT.