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A chemical, genetic, and structural analysis of the nuclear bile acid receptor fxr

Analyse A chemical, genetic, and structural analysis of the nuclear bile acid receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OSH
Type: protein
Length: 216 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile acid receptor
UniProt: Q96RI1
Ligands: FEX
Pockets: 2 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile acid receptor	protein	216	73% helix, 0% strand	Q96RI1

Ligands and binding sites

FEX · Methyl 3-{3-[(cyclohexylcarbonyl){[4'-(dimethylamino)biphenyl-4-yl]methyl}amino]phenyl}acrylate · 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	330	0.79	0.89	35	FEX
2	139	0.44	0.76	20	empty

Compared structures

1OSH · A Chemical, Genetic, and Structural Analysis of the nuclear bile acid receptor FXR · the same entry in another collection · chain A against A, TM-score 1.00
Q96RI1 · AlphaFold monomer V2.0 prediction for bile acid receptor (Q96RI1) · a predicted model of the same protein · chain A against A, TM-score 0.95

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
Elsewhere: RCSB PDB 1OSH · PDBe 1OSH · UniProt Q96RI1

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