Research workbench
AlphaFold monomer V2.0 prediction for N-acetylneuraminate epimerase (Q57QM5)
Analyse AlphaFold monomer V2.0 prediction for N-acetylneuraminate epimerase (Q57QM5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q57QM5
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- N-acetylneuraminate epimerase
- UniProt
- Q57QM5
- Pockets
- 2 · best druggability 0.79
Structure
1 distinct chain · 10% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylneuraminate epimerase | protein | 386 | 10% helix, 41% strand | Q57QM5 |
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 | 857 | 0.79 | 0.82 | 69 | empty |
| 2 | 76 | 0.37 | 0.77 | 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 Q57QM5
- Elsewhere: UniProt Q57QM5 · AlphaFold DB Q57QM5
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