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Crystal structure of human acetylcholinesterase

Analyse Crystal structure of human acetylcholinesterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7E3D
Type: protein
Length: 1,065 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylcholinesterase
EC: 3.1.1.7
UniProt: P22303
Ligands: NAG, FUC
Pockets: 16 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetylcholinesterase (EC 3.1.1.7)	protein	530	38% helix, 18% strand	P22303
B	Acetylcholinesterase (EC 3.1.1.7)	protein	535	38% helix, 18% strand	P22303

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, B
PE8 · 3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	269	0.75	0.88	35	empty
2	250	0.74	0.88	36	empty
3	344	0.60	0.77	35	empty
4	293	0.59	0.78	33	empty
5	147	0.58	0.83	20	empty

Interfaces

1 interface between chains.

A–B · 998 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

7E3D · Crystal structure of human acetylcholinesterase · the same entry in another collection · chain A against A, TM-score 1.00
P22303 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P22303) · a predicted model of the same protein · chain B 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 P22303
Elsewhere: RCSB PDB 7E3D · PDBe 7E3D · UniProt P22303

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