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Torpedo acetylcholinesterase - hg heavy-atom derivative

Analyse Torpedo acetylcholinesterase - hg heavy-atom derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J4F
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
Ligands: HG
Pockets: 3 · best druggability 0.74

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	527	38% helix, 16% strand	P04058

Ligands and binding sites

HG · Mercury (II) ion · metal · 2 copies · chains A

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

Pockets

3 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	273	0.74	0.87	38	empty
2	281	0.54	0.75	32	empty
3	76	0.36	0.76	19	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

2J4F · Torpedo acetylcholinesterase - Hg heavy-atom derivative · 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 2J4F · PDBe 2J4F · UniProt P04058

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