Research workbench

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: 5Q0I
Type: protein
Length: 239 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile acid receptor; Coactivator peptide pgc-1A ppar gamma coactivator
UniProt: Q96RI1, B7Z7E0
Ligands: 0X0
Pockets: 2 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile acid receptor	protein	227	72% helix, 0% strand	Q96RI1
B	Coactivator peptide pgc-1A ppar gamma coactivator	protein	12	58% helix, 0% strand	B7Z7E0

Ligands and binding sites

0X0 · 2-[(3,4-dimethoxyphenyl)-(4-methylphenyl)sulfonyl-amino]-N-(2,4-dimethylpentan-3-yl)ethanamide · 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	251	0.85	0.96	31	0X0
2	110	0.36	0.74	15	empty

Interfaces

1 interface between chains.

A–B · 560 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5Q0I · 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 B7Z7E0
Elsewhere: RCSB PDB 5Q0I · PDBe 5Q0I · UniProt Q96RI1 · UniProt B7Z7E0

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