MolNFT v1 · #139136 · protein

Crystal structure of acetylcholinesterase catalytic subunit of the malaria vector anopheles gambiae, 3.4 a

5X61: “Crystal structure of acetylcholinesterase catalytic subunit of the malaria vector anopheles gambiae, 3.4 a”. X-ray diffraction, 3 ligands (NAG, SO4, NH4), 13 pockets (best druggability 0.73). MolNFT v1 #139136 on GenesisL1: 3D…

PDB: 5X61
Type: protein
Length: 1,074 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetylcholinesterase
EC: 3.1.1.7
UniProt: Q869C3
Ligands: NAG, SO4, NH4
Pockets: 13 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Acetylcholinesterase (EC 3.1.1.7)	protein	537	36% helix, 17% strand	Q869C3

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains B, A
SO4 · Sulfate ion · ion · 16 copies · chains B, A
NH4 · Ammonium ion · ion · 2 copies · chains B, A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains B, A

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

Pockets

13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	300	0.73	0.85	37	NH4, EPE
2	330	0.72	0.84	37	SO4, NH4, EPE
3	58	0.64	0.94	21	empty
4	438	0.64	0.77	59	SO4
5	405	0.61	0.76	61	SO4

Interfaces

1 interface between chains.

B–A · 1457 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

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

Compared structures

5X61 · Crystal structure of Acetylcholinesterase Catalytic Subunit of the Malaria Vector… · the same entry in another collection · chain B against B, TM-score 1.00
Q869C3 · AlphaFold monomer V2.0 prediction for acetylcholinesterase (Q869C3) · 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 Q869C3
Elsewhere: RCSB PDB 5X61 · PDBe 5X61 · UniProt Q869C3

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.