Research workbench
AlphaFold monomer V2.0 prediction for nuclear protein localization protein 4 homolog (Q9ES54)
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
- Q9ES54
- Type
- protein
- Length
- 608 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xe3c96f8214BA49a269Bd99E09AE17503971805C1
- Molecule
- Nuclear protein localization protein 4 homolog
- UniProt
- Q9ES54
- Pockets
- 9 · best druggability 0.62
Structure
1 distinct chain · 23% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear protein localization protein 4 homolog | protein | 608 | 23% helix, 23% strand | Q9ES54 |
Pockets
9 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.62 | 0.82 | 34 | empty |
| 2 | 178 | 0.50 | 0.77 | 25 | empty |
| 3 | 53 | 0.49 | 0.87 | 15 | empty |
| 4 | 98 | 0.48 | 0.81 | 16 | empty |
| 5 | 149 | 0.46 | 0.77 | 27 | empty |
Compared structures
- 1Q5W · Ubiquitin Recognition by Npl4 Zinc-Fingers · an experimental structure of the same protein · chain A against A, TM-score 0.05
- 1Q5W · Ubiquitin recognition by NPL4 zinc-fingers · an experimental structure of the same protein · chain A against A, TM-score 0.05
- 1NJ3 · Structure and ubiquitin interactions of the conserved nzf domain of NPL4 · an experimental structure of the same protein · chain A against A, TM-score 0.05
- 1NJ3 · Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4 · an experimental structure of the same protein · chain A against A, TM-score 0.05
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 Q9ES54
- Elsewhere: UniProt Q9ES54 · AlphaFold DB Q9ES54
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