Research workbench
AlphaFold monomer V2.0 prediction for nuclear receptor-binding protein homolog (Q297L2)
Analyse AlphaFold monomer V2.0 prediction for nuclear receptor-binding protein homolog… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q297L2
- Type
- protein
- Length
- 663 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Nuclear receptor-binding protein homolog
- UniProt
- Q297L2
- Pockets
- 7 · best druggability 0.71
Structure
1 distinct chain · 31% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear receptor-binding protein homolog | protein | 663 | 31% helix, 14% strand | Q297L2 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 564 | 0.71 | 0.80 | 69 | empty |
| 2 | 141 | 0.67 | 0.88 | 25 | empty |
| 3 | 173 | 0.51 | 0.78 | 22 | empty |
| 4 | 151 | 0.46 | 0.76 | 19 | empty |
| 5 | 147 | 0.44 | 0.75 | 22 | empty |
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 Q297L2
- Elsewhere: UniProt Q297L2 · AlphaFold DB Q297L2
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