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Structure of human fxr in complex with mfa-1 and co-activator peptide

Analyse Structure of human fxr in complex with mfa-1 and co-activator peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BEJ
Type: protein
Length: 475 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bile acid receptor; Nuclear receptor coactivator 1
UniProt: Q96RI1, Q15788
Ligands: MUF, YT3
Pockets: 7 · best druggability 0.81

Structure

x-ray diffraction · 4 distinct chains · 72% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bile acid receptor	protein	224	74% helix, 0% strand	Q96RI1
B	Bile acid receptor	protein	228	71% helix, 0% strand	Q96RI1
E	Nuclear receptor coactivator 1	protein	11	55% helix, 0% strand	Q15788
F	Nuclear receptor coactivator 1	protein	12	58% helix, 0% strand	Q15788

Ligands and binding sites

MUF · (8alpha,10alpha,13alpha,17beta)-17-[(4-hydroxyphenyl)carbonyl]androsta-3,5-diene-3-carboxylic acid · ligand · 2 copies · chains A, B
YT3 · Yttrium (III) ion · metal · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	417	0.81	0.89	41	MUF
2	401	0.79	0.88	47	MUF
3	1149	0.77	0.79	63	empty
4	63	0.59	0.90	16	empty
5	92	0.46	0.80	15	empty

Interfaces

3 interfaces between chains.

A–E · 694 Å² buried · 10 hydrogen bonds · protein-protein
A–B · 604 Å² buried · 13 hydrogen bonds · protein-protein
B–F · 597 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

3BEJ · Structure of human FXR in complex with MFA-1 and co-activator peptide · 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
Every structure of UniProt Q15788
Elsewhere: RCSB PDB 3BEJ · PDBe 3BEJ · UniProt Q96RI1 · UniProt Q15788

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