Research workbench
Structural insight of the molecular mechanism of cilofexor bound to fxr
Analyse Structural insight of the molecular mechanism of cilofexor bound to fxr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VUE
- Type
- protein
- Length
- 237 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96RI1, Q15596
- Ligands
- 811
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 226 | — | Q96RI1 |
| B | — | protein | 11 | — | Q15596 |
Ligands and binding sites
- 811 · 2-[3-[4-[[3-[2,6-bis(chloranyl)phenyl]-5-cyclopropyl-1, 2-oxazol-4-yl]methoxy]-2-chloranyl-phenyl]-3-oxidanyl-azetidin-1-yl]pyridine-4-carboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7VUE · Structural insight of the molecular mechanism of cilofexor bound to FXR · 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 Q15596
- Elsewhere: RCSB PDB 7VUE · PDBe 7VUE · UniProt Q96RI1 · UniProt Q15596
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