Research workbench
AlphaFold monomer V2.0 prediction for ADP-dependent (S)-NAD(P)H-hydrate dehydratase (A0RU82)
Analyse AlphaFold monomer V2.0 prediction for ADP-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
- A0RU82
- Type
- protein
- Length
- 287 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9a3d3E3c804559Ff57D6bdF22acA278B4f92e6F7
- Molecule
- ADP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- A0RU82
- Pockets
- 2 · best druggability 0.53
Structure
1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 287 | 47% helix, 16% strand | A0RU82 |
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 | 103 | 0.53 | 0.83 | 21 | empty |
| 2 | 131 | 0.44 | 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 A0RU82
- Elsewhere: UniProt A0RU82 · AlphaFold DB A0RU82
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