MolNFT v1 · #131304 · protein

Ligand binding to farnesoid-X-receptor

5Q17 · Bile acid receptor: “Ligand binding to farnesoid-X-receptor”. X-ray diffraction, 1 ligand (9MV), 2 pockets (best druggability 0.82). MolNFT v1 #131304 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5Q17
Type: protein
Length: 236 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile acid receptor; Nuclear receptor coactivator peptide SRC2
UniProt: Q96RI1, A0A0B6XJZ8
Ligands: 9MV
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile acid receptor	protein	224	75% helix, 0% strand	Q96RI1
B	Nuclear receptor coactivator peptide SRC2	protein	12	58% helix, 0% strand	A0A0B6XJZ8

Ligands and binding sites

9MV · 4-({5-bromo-2-oxo-1'-[(thiophen-2-yl) sulfonyl]spiro[indole-3,4'-piperidin]-1(2H)-yl}methyl)benzoic 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	407	0.82	0.90	46	9MV
2	131	0.42	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 553 Å² buried · 4 hydrogen bonds · protein-protein

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 A0A0B6XJZ8
Elsewhere: RCSB PDB 5Q17 · PDBe 5Q17 · UniProt Q96RI1 · UniProt A0A0B6XJZ8

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