Research workbench
AlphaFold monomer V2.0 prediction for nuclear receptor subfamily 2 group F member 6 (P10588)
Analyse AlphaFold monomer V2.0 prediction for nuclear receptor subfamily 2 group F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P10588
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8a5dA748134251361a203fcC5f1E49CB75628D2C
- Molecule
- Nuclear receptor subfamily 2 group F member 6
- UniProt
- P10588
- Pockets
- 3 · best druggability 0.59
Structure
1 distinct chain · 45% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear receptor subfamily 2 group F member 6 | protein | 404 | 45% helix, 1% strand | P10588 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.59 | 0.84 | 21 | empty |
| 2 | 73 | 0.32 | 0.74 | 13 | empty |
| 3 | 50 | 0.25 | 0.73 | 12 | empty |
Compared structures
- 8C5L · NR2F6 ligand binding domain in complex with NSD1 peptide · an experimental structure of the same protein · chain A against B, TM-score 0.47
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 P10588
- Elsewhere: UniProt P10588 · AlphaFold DB P10588
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