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Specific chemical and structural damage at nine time points (point F) caused by intense synchrotron radiation to torpedo californica acetylcholinesterase

Analyse Specific chemical and structural damage at nine time points (point F) caused by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QII
Type: protein
Length: 532 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.65
Source: Torpedo californica
Molecule: Acetylcholinesterase
EC: 3.1.1.7
UniProt: P04058
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · resolution 2.65 · 1 distinct chain · 38% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetylcholinesterase (EC 3.1.1.7)	protein	532	38% helix, 16% strand	P04058

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	386	0.77	0.86	35	empty
2	317	0.56	0.76	32	empty
3	114	0.42	0.76	15	empty
4	64	0.34	0.77	14	empty
5	73	0.33	0.75	15	empty

Compared structures

1QII · Specific chemical and structural damage at nine time points (point F) caused by intense… · the same entry in another collection · chain A against A, TM-score 1.00
P04058 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P04058) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P04058
Elsewhere: RCSB PDB 1QII · PDBe 1QII · UniProt P04058

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