Research workbench

Crystal structure of acetylcholine binding protein complexed with metocurine

Analyse Crystal structure of acetylcholine binding protein complexed with metocurine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PEO
Type: protein
Length: 2,062 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Soluble acetylcholine receptor
UniProt: Q8WSF8
Ligands: CU9
Pockets: 20 · best druggability 0.71

Structure

x-ray diffraction · 8 distinct chains · 9% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Soluble acetylcholine receptor	protein	203	7% helix, 54% strand	Q8WSF8
B	Soluble acetylcholine receptor	protein	208	11% helix, 50% strand	Q8WSF8
C, H	Soluble acetylcholine receptor	protein	211	12% helix, 49% strand	Q8WSF8
D, I	Soluble acetylcholine receptor	protein	204	8% helix, 52% strand	Q8WSF8
E	Soluble acetylcholine receptor	protein	205	8% helix, 50% strand	Q8WSF8
F	Soluble acetylcholine receptor	protein	202	8% helix, 50% strand	Q8WSF8
G	Soluble acetylcholine receptor	protein	207	11% helix, 51% strand	Q8WSF8
J	Soluble acetylcholine receptor	protein	207	8% helix, 50% strand	Q8WSF8

Ligands and binding sites

CU9 · 6,6',7',12'-tetramethoxy-2,2,2',2'-tetramethyltubocuraran-2,2'-diium · ligand · 8 copies · chains A, E, B, C, D, F, G, J, H, I

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	611	0.71	0.79	63	CU9
2	588	0.69	0.78	63	CU9
3	634	0.69	0.77	71	empty
4	536	0.68	0.78	49	CU9
5	612	0.67	0.77	60	CU9

Interfaces

13 interfaces between chains.

F–G · 1385 Å² buried · 18 hydrogen bonds · protein-protein
G–H · 1377 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 1375 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1370 Å² buried · 16 hydrogen bonds · protein-protein
F–J · 1300 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

Compared structures

3PEO · Crystal structure of acetylcholine binding protein complexed with metocurine · the same entry in another collection · 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 Q8WSF8
Elsewhere: RCSB PDB 3PEO · PDBe 3PEO · UniProt Q8WSF8

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