MolNFT v1 · #114518 · protein

X-ray crystal structure of aplysia californica (ac-achbp) in complex with 2-pyridyl AZATRICYCLO[3.3.1.13,7]DECANE; 2-pyridylazaadamantane; 2-aza (ti-8480)

5BRX · Soluble acetylcholine receptor: “X-ray crystal structure of aplysia californica (ac-achbp) in complex with 2-pyridyl…”. X-ray diffraction, 2 ligands (TI4, SO4), 20 pockets (best druggability 0.79). MolNFT v1 #114518 on GenesisL1: 3D…

PDB: 5BRX
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: TI4, SO4
Pockets: 20 · best druggability 0.79

Structure

x-ray diffraction · 6 distinct chains · 12% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Soluble acetylcholine receptor	protein	209	11% helix, 53% strand	Q8WSF8
B, G	Soluble acetylcholine receptor	protein	212	12% helix, 49% strand	Q8WSF8
D, I	Soluble acetylcholine receptor	protein	214	13% helix, 49% strand	Q8WSF8
E, J	Soluble acetylcholine receptor	protein	209	11% helix, 49% strand	Q8WSF8
F	Soluble acetylcholine receptor	protein	209	12% helix, 53% strand	Q8WSF8
H	Soluble acetylcholine receptor	protein	208	11% helix, 50% strand	Q8WSF8

Ligands and binding sites

TI4 · (2R,3S,5R,7S)-2-(pyridin-3-yl)-1-azatricyclo[3.3.1.1~3,7~]decane · ligand · 4 copies · chains A, E, C, D, F, J, H, I
SO4 · Sulfate ion · ion · 10 copies · chains A, B, E, C, D, F, G, J, H, I
PG4 · Tetraethylene glycol · additive · 6 copies · chains A, B, C, D, E, F, G, H, I, 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	1197	0.79	0.80	150	empty
2	654	0.75	0.81	78	empty
3	493	0.72	0.81	56	empty
4	448	0.70	0.81	58	empty
5	271	0.69	0.84	47	TI4

Interfaces

20 interfaces between chains.

C–D · 1436 Å² buried · 15 hydrogen bonds · protein-protein
H–I · 1435 Å² buried · 16 hydrogen bonds · protein-protein
A–E · 1427 Å² buried · 16 hydrogen bonds · protein-protein
F–J · 1411 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 1289 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

Compared structures

5BRX · X-ray crystal structure of Aplysia californica (Ac-AChBP) in complex with 2-pyridyl… · 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 5BRX · PDBe 5BRX · UniProt Q8WSF8

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