Research workbench
AlphaFold monomer V2.0 prediction for oxidoreductase NAD-binding domain-containing protein 1 (Q8VE38)
Analyse AlphaFold monomer V2.0 prediction for oxidoreductase NAD-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8VE38
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Oxidoreductase NAD-binding domain-containing protein 1
- UniProt
- Q8VE38
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 25% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxidoreductase NAD-binding domain-containing protein 1 | protein | 311 | 25% helix, 28% strand | Q8VE38 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 327 | 0.64 | 0.79 | 47 | empty |
| 2 | 96 | 0.37 | 0.76 | 14 | empty |
| 3 | 70 | 0.34 | 0.76 | 13 | empty |
| 4 | 81 | 0.34 | 0.75 | 17 | 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 Q8VE38
- Elsewhere: UniProt Q8VE38 · AlphaFold DB Q8VE38
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