MolNFT v1 · #110030 · protein

Crystal structure of a-achbp in complex with pinnatoxin G

4XK9 · Soluble acetylcholine receptor: “Crystal structure of a-achbp in complex with pinnatoxin G”. X-ray diffraction, 2 ligands (41J, CL), 20 pockets (best druggability 0.68). MolNFT v1 #110030 on GenesisL1: 3D structure, binding sites…

PDB: 4XK9
Type: protein
Length: 2,105 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Soluble acetylcholine receptor
UniProt: Q8WSF8
Ligands: 41J, CL
Pockets: 20 · best druggability 0.68

Structure

x-ray diffraction · 7 distinct chains · 10% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Soluble acetylcholine receptor	protein	210	10% helix, 49% strand	Q8WSF8
B	Soluble acetylcholine receptor	protein	213	12% helix, 48% strand	Q8WSF8
C	Soluble acetylcholine receptor	protein	209	10% helix, 49% strand	Q8WSF8
D	Soluble acetylcholine receptor	protein	207	9% helix, 50% strand	Q8WSF8
E, H, J	Soluble acetylcholine receptor	protein	212	11% helix, 49% strand	Q8WSF8
F, I	Soluble acetylcholine receptor	protein	211	10% helix, 49% strand	Q8WSF8
G	Soluble acetylcholine receptor	protein	208	10% helix, 50% strand	Q8WSF8

Ligands and binding sites

41J · Pinnatoxin G · ligand · 10 copies · chains A, E, B, C, D, F, J, G, H, I
CL · Chloride ion · ion · 7 copies · chains A, B, C, E, G, H, J

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	624	0.68	0.77	52	41J
2	589	0.67	0.77	46	41J
3	624	0.67	0.77	61	41J
4	593	0.66	0.76	44	41J
5	530	0.66	0.77	51	41J

Interfaces

12 interfaces between chains.

F–G · 1406 Å² buried · 22 hydrogen bonds · protein-protein
F–J · 1406 Å² buried · 21 hydrogen bonds · protein-protein
H–I · 1375 Å² buried · 20 hydrogen bonds · protein-protein
A–E · 1374 Å² buried · 18 hydrogen bonds · protein-protein
I–J · 1364 Å² buried · 21 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

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 4XK9 · PDBe 4XK9 · UniProt Q8WSF8

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