MolNFT v1 · #25353 · protein

Acetylcholinesterase (E.C. 3.1.1.7) complexed with huperzine a

1VOT: “Acetylcholinesterase (E.C. 3.1.1.7) complexed with huperzine a”. X-ray diffraction, 1 ligand (HUP), 4 pockets (best druggability 0.76). MolNFT v1 #25353 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1VOT
Type: protein
Length: 529 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylcholinesterase
EC: 3.1.1.7
UniProt: P04058
Ligands: HUP
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetylcholinesterase (EC 3.1.1.7)	protein	529	38% helix, 17% strand	P04058

Ligands and binding sites

HUP · Huperzine A · ligand · chains A

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

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	294	0.76	0.88	40	HUP
2	305	0.55	0.75	32	empty
3	83	0.39	0.77	14	empty
4	51	0.31	0.77	12	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1VOT · Acetylcholinesterase (E.C. 3.1.1.7) complexed with huperzine a · 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 1VOT · PDBe 1VOT · UniProt P04058

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