Research workbench
AlphaFold monomer V2.0 prediction for nuclear protein localization protein 4 homolog (Q9VBP9)
Analyse AlphaFold monomer V2.0 prediction for nuclear protein localization protein 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9VBP9
- Type
- protein
- Length
- 652 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Nuclear protein localization protein 4 homolog
- UniProt
- Q9VBP9
- Pockets
- 10 · best druggability 0.65
Structure
1 distinct chain · 27% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear protein localization protein 4 homolog | protein | 652 | 27% helix, 20% strand | Q9VBP9 |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.65 | 0.83 | 36 | empty |
| 2 | 245 | 0.55 | 0.78 | 20 | empty |
| 3 | 235 | 0.54 | 0.77 | 28 | empty |
| 4 | 222 | 0.50 | 0.75 | 31 | empty |
| 5 | 154 | 0.50 | 0.78 | 25 | empty |
Compared structures
- 4RV0 · Crystal structure of tn complex · an experimental structure of the same protein · chain A against B, TM-score 0.11
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 Q9VBP9
- Elsewhere: UniProt Q9VBP9 · AlphaFold DB Q9VBP9
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