MolNFT v1 · #131313 · protein

Ligand binding to farnesoid-X-receptor

5Q1G · Bile acid receptor: “Ligand binding to farnesoid-X-receptor”. X-ray diffraction, 1 ligand (9NM), 3 pockets (best druggability 0.83). MolNFT v1 #131313 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5Q1G
Type: protein
Length: 233 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: 9NM
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile acid receptor	protein	224	70% helix, 0% strand	Q96RI1
B	Coactivator peptide src-1 HD3	protein	9	78% helix, 0% strand	A8K1V4

Ligands and binding sites

9NM · (2E)-N-cyclohexyl-N-(cyclohexylcarbamoyl)-3-(4-fluorophenyl)prop-2-enamide · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	231	0.83	0.95	31	9NM
2	98	0.52	0.83	20	empty
3	126	0.40	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 556 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5Q1G · 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 5Q1G · PDBe 5Q1G · UniProt Q96RI1 · UniProt A8K1V4

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