Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-hydrate epimerase (A5VML0)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-hydrate epimerase (A5VML0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VML0
- Type
- protein
- Length
- 212 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2815ad069368e5711A082F851Ff644B6454E18F2
- Molecule
- NAD(P)H-hydrate epimerase
- UniProt
- A5VML0
- Pockets
- 1 · best druggability 0.64
Structure
1 distinct chain · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-hydrate epimerase | protein | 212 | 42% helix, 18% strand | A5VML0 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.64 | 0.80 | 33 | 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 A5VML0
- Elsewhere: UniProt A5VML0 · AlphaFold DB A5VML0
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