domain_motion

How a domain turns and shifts between two structures, after superposing on a fixed part.

from proteinmotion import domain_motion

Signature

domain_motion(source, target, moving, fixed=None, *, match=None)

Parameters

Parameter	Default	Description
`source`	Required	Structure that defines the regions and the frame of the result.
`target`	Required	Second structure of the same protein.
`moving`	Required	Region of the source whose motion is measured.
`fixed`	`None`	Region of the source used to superpose the target; None uses all matched trace atoms.
`match`keyword only	`None`	StructureMatch to reuse; None calls match_structures().

Returns: DomainMotion

Example and output

Run this command from a repository checkout.

Code Render command

proteinmotion render examples/structure_morph.py AdenylateKinaseMorph \
  -o adenylate-kinase-morph.mp4 --fps 60

Output Preview · 17.2 s · 60 fps

Adenylate kinase closes

Open adenylate kinase (4AKE) closes around the inhibitor Ap5A (1AKE), superposed on the CORE. The LID turns 52° and the NMP-binding domain 45°; a ruler between them shortens from 43.7 Å to 19.1 Å, and Ap5A, present only in 1AKE, fades in.

Full source: AdenylateKinaseMorph Download MP4