Research workbench
AlphaFold monomer V2.0 prediction for nuclear valosin-containing protein-like (O15381)
Analyse AlphaFold monomer V2.0 prediction for nuclear valosin-containing protein-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O15381
- Type
- protein
- Length
- 856 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Nuclear valosin-containing protein-like
- UniProt
- O15381
- Pockets
- 9 · best druggability 0.58
Structure
1 distinct chain · 46% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear valosin-containing protein-like | protein | 856 | 46% helix, 7% strand | O15381 |
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.58 | 0.80 | 35 | empty |
| 2 | 151 | 0.56 | 0.82 | 32 | empty |
| 3 | 227 | 0.50 | 0.75 | 28 | empty |
| 4 | 104 | 0.48 | 0.80 | 22 | empty |
| 5 | 143 | 0.44 | 0.76 | 20 | empty |
Compared structures
- 2X8A · Human Nuclear Valosin containing protein Like (NVL), C-terminal AAA- ATPase domain · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 2X8A · Human nuclear valosin containing protein like (nvl), C- terminal aaa-ATPase domain · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 6RO1 · X-ray crystal structure of the MTR4 nvl complex · an experimental structure of the same protein · chain A against B, TM-score 0.02
- 6RO1 · X-ray crystal structure of the MTR4 NVL complex · an experimental structure of the same protein · chain A against B, TM-score 0.02
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 O15381
- Elsewhere: UniProt O15381 · AlphaFold DB O15381
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