Research workbench
AlphaFold monomer V2.0 prediction for N-acetylneuraminate epimerase (A5VU94)
Analyse AlphaFold monomer V2.0 prediction for N-acetylneuraminate epimerase (A5VU94) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VU94
- Type
- protein
- Length
- 388 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- N-acetylneuraminate epimerase
- UniProt
- A5VU94
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 11% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylneuraminate epimerase | protein | 388 | 11% helix, 40% strand | A5VU94 |
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 | 731 | 0.76 | 0.81 | 73 | empty |
| 2 | 67 | 0.42 | 0.81 | 16 | 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 A5VU94
- Elsewhere: UniProt A5VU94 · AlphaFold DB A5VU94
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