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Crystal structure of mutant achbp in complex with strychnine (T53F, Q74R, Y110A, I135S, G162E)

Analyse Crystal structure of mutant achbp in complex with strychnine (T53F, Q74R… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5OAL
Type: protein
Length: 3,078 residues
Chains: 15
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Soluble acetylcholine receptor
UniProt: Q8WSF8
Ligands: SY9, ARG
Pockets: 20 · best druggability 0.75

Structure

x-ray diffraction · 5 distinct chains · 7% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, F, H, I, J, K, L, M, O	Soluble acetylcholine receptor	protein	206	8% helix, 55% strand	Q8WSF8
B, C	Soluble acetylcholine receptor	protein	207	8% helix, 55% strand	Q8WSF8
E	Soluble acetylcholine receptor	protein	204	8% helix, 55% strand	Q8WSF8
G	Soluble acetylcholine receptor	protein	202	8% helix, 53% strand	Q8WSF8
N	Soluble acetylcholine receptor	protein	198	6% helix, 58% strand	Q8WSF8

Ligands and binding sites

SY9 · Strychnine · ligand · 15 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, O, M, N
ARG · Arginine · ligand · chains N

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	503	0.75	0.83	51	empty
2	495	0.74	0.83	52	SY9
3	498	0.74	0.83	46	SY9
4	513	0.73	0.82	44	SY9
5	460	0.73	0.83	53	SY9

Interfaces

25 interfaces between chains.

I–J · 1414 Å² buried · 18 hydrogen bonds · protein-protein
L–M · 1363 Å² buried · 18 hydrogen bonds · protein-protein
F–J · 1348 Å² buried · 18 hydrogen bonds · protein-protein
M–N · 1341 Å² buried · 16 hydrogen bonds · protein-protein
H–I · 1332 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 29 disulfide (disulfide).

Compared structures

5OAL · Crystal structure of mutant AChBP in complex with strychnine (T53F, Q74R, Y110A, I135S… · 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 5OAL · PDBe 5OAL · UniProt Q8WSF8

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