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AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate dehydratase (P36059)
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
- P36059
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE651A2B061FB7771bFB843238E8B9bBBaaA9AbbC
- Molecule
- ATP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- P36059
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 337 | 52% helix, 12% strand | P36059 |
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 | 250 | 0.52 | 0.76 | 34 | empty |
| 2 | 66 | 0.41 | 0.80 | 17 | empty |
| 3 | 75 | 0.34 | 0.75 | 11 | empty |
| 4 | 56 | 0.29 | 0.74 | 18 | 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 P36059
- Elsewhere: UniProt P36059 · AlphaFold DB P36059
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