Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate dehydratase (B7FXE8)
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
- B7FXE8
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaa53776A41fB2e67da75A96E8a53746b6874aAB4
- Molecule
- ATP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- B7FXE8
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 310 | 48% helix, 15% strand | B7FXE8 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.56 | 0.80 | 32 | empty |
| 2 | 83 | 0.44 | 0.80 | 21 | empty |
| 3 | 67 | 0.33 | 0.75 | 15 | 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 B7FXE8
- Elsewhere: UniProt B7FXE8 · AlphaFold DB B7FXE8
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