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O-methylphosphorylated torpedo acetylcholinesterase obtained by reaction with methyl paraoxon (aged)

Analyse O-methylphosphorylated torpedo acetylcholinesterase obtained by reaction with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GEL
Type: protein
Length: 527 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: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetylcholinesterase (EC 3.1.1.7)	protein	527	39% helix, 18% strand	P04058

Pockets

4 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	314	0.75	0.86	37	empty
2	344	0.57	0.76	34	empty
3	114	0.45	0.78	22	empty
4	67	0.35	0.77	14	empty

Modifications

Observed in the structure: 3 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

3GEL · O-Methylphosphorylated Torpedo Acetylcholinesterase Obtained by Reaction with Methyl… · 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 3GEL · PDBe 3GEL · UniProt P04058

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