Research workbench
AlphaFold monomer V2.0 prediction for ADP-dependent (S)-NAD(P)H-hydrate dehydratase (A6GXW4)
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
- A6GXW4
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xeBF61c568fBcb94886aEe7A219fA8A13e3ABEa19
- Molecule
- ADP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- A6GXW4
- Pockets
- 1 · best druggability 0.43
Structure
1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 282 | 48% helix, 14% strand | A6GXW4 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.43 | 0.76 | 31 | 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 A6GXW4
- Elsewhere: UniProt A6GXW4 · AlphaFold DB A6GXW4
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