MolNFT v1 · #131281 · protein
Ligand binding to farnesoid-X-receptor
5Q0K · Bile acid receptor: “Ligand binding to farnesoid-X-receptor”. X-ray diffraction, 2 pockets (best druggability 0.82). MolNFT v1 #131281 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5Q0K
- Type
- protein
- Length
- 237 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
- 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 | 76% helix, 0% strand | Q96RI1 |
| B | Coactivator peptide src-1 HD3 | protein | 13 | 54% helix, 0% strand | A8K1V4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.82 | 0.91 | 45 | empty |
| 2 | 107 | 0.38 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 609 Ų buried · 7 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 A8K1V4
- Elsewhere: RCSB PDB 5Q0K · PDBe 5Q0K · UniProt Q96RI1 · UniProt A8K1V4
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