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Ligand binding to farnesoid-X-receptor

Analyse Ligand binding to farnesoid-X-receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5Q0X
Type: protein
Length: 235 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile acid receptor; Coactivator peptide src-1 HD3
UniProt: Q96RI1, A8K1V4
Ligands: 643
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile acid receptor	protein	222	74% helix, 0% strand	Q96RI1
B	Coactivator peptide src-1 HD3	protein	13	62% helix, 0% strand	A8K1V4

Ligands and binding sites

643 · 6-(4-{[3-(3,5-dichloropyridin-4-yl)-5-(1-methylethyl) isoxazol-4-yl]methoxy}-2-methylphenyl)-1-methyl-1H-indole-3-carbox ylic acid · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	390	0.78	0.87	42	643
2	136	0.42	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 606 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

5Q0X · Ligand binding to FARNESOID-X-RECEPTOR · 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 Q96RI1
Every structure of UniProt A8K1V4
Elsewhere: RCSB PDB 5Q0X · PDBe 5Q0X · UniProt Q96RI1 · UniProt A8K1V4

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