Research workbench

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

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

PDB: 1QIG
Type: protein
Length: 532 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylcholinesterase
EC: 3.1.1.7
UniProt: P04058
Pockets: 5 · best druggability 0.77

Structure

x-ray diffraction · 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

5 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	370	0.77	0.87	37	empty
2	325	0.56	0.76	31	empty
3	103	0.41	0.76	14	empty
4	71	0.35	0.76	14	empty
5	60	0.34	0.77	14	empty

Compared structures

1QIG · Specific chemical and structural damage at nine time points (point D) 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 1QIG · PDBe 1QIG · UniProt P04058

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