Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 2-epimerase (H2VFI5)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 2-epimerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- H2VFI5
- Type
- protein
- Length
- 377 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xFb1Fd01bBa777F5321d3CeBE17CEDAC28290Fb4D
- Molecule
- Udp-N-acetylglucosamine 2-epimerase
- UniProt
- H2VFI5
- Pockets
- 3 · best druggability 0.82
Structure
1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 2-epimerase | protein | 377 | 45% helix, 16% strand | H2VFI5 |
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 | 234 | 0.82 | 0.95 | 35 | empty |
| 2 | 98 | 0.49 | 0.82 | 25 | empty |
| 3 | 55 | 0.44 | 0.83 | 12 | 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 H2VFI5
- Elsewhere: UniProt H2VFI5 · AlphaFold DB H2VFI5
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