Research workbench
Fxr with cdca and ncoa-2 peptide
Analyse Fxr with cdca and ncoa-2 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QE6
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bile acid receptor; Nuclear receptor coactivator 2
- UniProt
- Q96RI1, Q15596
- Ligands
- JN3
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bile acid receptor | protein | 228 | 70% helix, 0% strand | Q96RI1 |
| B | Nuclear receptor coactivator 2 | protein | 13 | 62% helix, 0% strand | Q15596 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 468 | 0.83 | 0.90 | 53 | JN3 |
| 2 | 187 | 0.49 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 624 Ų buried · 12 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 Q15596
- Elsewhere: RCSB PDB 4QE6 · PDBe 4QE6 · UniProt Q96RI1 · UniProt Q15596
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