MolNFT v1 · #266454 · protein
AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate dehydratase (Q17NP0)
Q17NP0: “AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate dehydratase (Q17NP0)”. 3 pockets (best druggability 0.56). MolNFT v1 #266454 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q17NP0
- Type
- protein
- Length
- 332 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3F7c838ccc23133e72aA1c8841D2c157C4B4810a
- Molecule
- ATP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- Q17NP0
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 45% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 332 | 45% helix, 12% strand | Q17NP0 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.56 | 0.77 | 34 | empty |
| 2 | 205 | 0.50 | 0.76 | 25 | empty |
| 3 | 67 | 0.32 | 0.75 | 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 Q17NP0
- Elsewhere: UniProt Q17NP0 · AlphaFold DB Q17NP0
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