Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate dehydratase (Q9VVW8)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9VVW8
- Type
- protein
- Length
- 300 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x934f84D099E5FEaBA89bC58DBEB7366EFF6BF871
- Molecule
- ATP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- Q9VVW8
- Pockets
- 3 · best druggability 0.54
Structure
1 distinct chain · 50% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 300 | 50% helix, 15% strand | Q9VVW8 |
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 | 215 | 0.54 | 0.78 | 35 | empty |
| 2 | 79 | 0.36 | 0.76 | 13 | empty |
| 3 | 55 | 0.30 | 0.76 | 16 | 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 Q9VVW8
- Elsewhere: UniProt Q9VVW8 · AlphaFold DB Q9VVW8
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