Research workbench
Crystal structure of human fxr in complex with 4-({(2S)-2-[2-(4- chlorophenyl)-5,6-difluoro-1H-benzimidazol-1-yl]-2- CYCLOHEXYLACETYL}AMINO)BENZOIC acid
Analyse Crystal structure of human fxr in complex with 4-({(2S)-2-[2-(4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OOF
- Type
- protein
- Length
- 485 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bile acid receptor; Peptide of nuclear receptor coactivator 1
- UniProt
- Q96RI1, Q15788
- Ligands
- OOF
- Pockets
- 6 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Bile acid receptor | protein | 230 | 72% helix, 0% strand | Q96RI1 |
| B | Peptide of nuclear receptor coactivator 1 | protein | 12 | 67% helix, 0% strand | Q15788 |
| D | Peptide of nuclear receptor coactivator 1 | protein | 13 | 62% helix, 0% strand | Q15788 |
Ligands and binding sites
- OOF · 4-({(2S)-2-[2-(4-chlorophenyl)-5,6-difluoro-1H-benzimidazol-1-yl]-2-cyclohexylacetyl}amino)benzoic acid · ligand · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 326 | 0.85 | 0.94 | 36 | OOF |
| 2 | 284 | 0.85 | 0.95 | 36 | OOF |
| 3 | 871 | 0.78 | 0.81 | 75 | empty |
| 4 | 207 | 0.54 | 0.78 | 21 | empty |
| 5 | 85 | 0.35 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1052 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 636 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 584 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 3OOF · PDBe 3OOF · UniProt Q96RI1 · UniProt Q15788
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