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Aged form of mouse acetylcholinesterase inhibited by tabun- update

Analyse Aged form of mouse acetylcholinesterase inhibited by tabun- update in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DL7
Type: protein
Length: 1,069 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylcholinesterase
EC: 3.1.1.7
UniProt: P21836
Ligands: NAG, CL
Pockets: 14 · best druggability 0.76

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	537	39% helix, 18% strand	P21836
B	Acetylcholinesterase (EC 3.1.1.7)	protein	532	38% helix, 19% strand	P21836

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
CL · Chloride ion · ion · chains A
P6G · Hexaethylene glycol · additive · chains A, B
PG4 · Tetraethylene glycol · additive · chains A, B

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

Pockets

14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	280	0.76	0.88	35	empty
2	293	0.74	0.87	37	empty
3	182	0.65	0.85	26	P6G
4	336	0.61	0.78	34	empty
5	147	0.56	0.82	18	empty

Interfaces

1 interface between chains.

A–B · 964 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 2 modified, 1 glycan (disulfide, nonstandard, N-glycosylation).

Compared structures

3DL7 · Aged Form of Mouse Acetylcholinesterase Inhibited by Tabun- Update · the same entry in another collection · chain B against B, TM-score 1.00
P21836 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (P21836) · 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 P21836
Elsewhere: RCSB PDB 3DL7 · PDBe 3DL7 · UniProt P21836

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