Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-hydrate epimerase (Q5X170)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-hydrate epimerase (Q5X170) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5X170
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD0B8f00ed836787a27f2236104D09DdB625B883a
- Molecule
- NAD(P)H-hydrate epimerase
- UniProt
- Q5X170
- Pockets
- 5 · best druggability 0.59
Structure
1 distinct chain · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-hydrate epimerase | protein | 270 | 34% helix, 19% strand | Q5X170 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.59 | 0.79 | 40 | empty |
| 2 | 118 | 0.55 | 0.83 | 21 | empty |
| 3 | 51 | 0.45 | 0.84 | 16 | empty |
| 4 | 70 | 0.36 | 0.77 | 14 | empty |
| 5 | 55 | 0.28 | 0.74 | 13 | 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 Q5X170
- Elsewhere: UniProt Q5X170 · AlphaFold DB Q5X170
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