Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate dehydratase (A8N8Z0)
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
- A8N8Z0
- Type
- protein
- Length
- 336 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- ATP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- A8N8Z0
- Pockets
- 2 · best druggability 0.51
Structure
1 distinct chain · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 336 | 47% helix, 12% strand | A8N8Z0 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 229 | 0.51 | 0.76 | 37 | empty |
| 2 | 129 | 0.45 | 0.77 | 21 | 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 A8N8Z0
- Elsewhere: UniProt A8N8Z0 · AlphaFold DB A8N8Z0
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