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
- 5Q0Z
- Type
- protein
- Length
- 482 residues
- Chains
- 4
- 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
- 9M1
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Bile acid receptor | protein | 230 | 70% helix, 0% strand | Q96RI1 |
| B, D | Coactivator peptide src-1 HD3 | protein | 11 | 73% helix, 0% strand | A8K1V4 |
Ligands and binding sites
- 9M1 · ethyl (5S)-3-(3,4-difluorobenzene-1-carbonyl)-1,1-dimethyl-1,2,3,4,5,6-hexahydroazepino[4,5-b]indole-5-carboxylate · ligand · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 281 | 0.86 | 0.96 | 36 | 9M1 |
| 2 | 223 | 0.84 | 0.96 | 33 | 9M1 |
| 3 | 200 | 0.47 | 0.75 | 29 | empty |
| 4 | 150 | 0.43 | 0.75 | 18 | empty |
| 5 | 117 | 0.39 | 0.75 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–B · 601 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 594 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 147 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5Q0Z · 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 5Q0Z · PDBe 5Q0Z · UniProt Q96RI1 · UniProt A8K1V4
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