MolNFT v1 · #63829 · protein
Discovery of XL335, a highly potent, selective and orally- active agonist of the farnesoid X receptor (fxr)
3FLI: “Discovery of XL335, a highly potent, selective and orally- active agonist of the farnesoid X receptor (fxr)”. X-ray diffraction. MolNFT v1 #63829 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FLI
- Type
- protein
- Length
- 221 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96RI1
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 221 | — | Q96RI1 |
Compared structures
- 3FLI · Discovery of XL335, a Highly Potent, Selective and Orally-Active Agonist of the Farnesoid… · 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 0.96
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
- Elsewhere: RCSB PDB 3FLI · PDBe 3FLI · UniProt Q96RI1
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