Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (Q7P0X5)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7P0X5
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf946795cBBF0d709882f916b7A64276982c26588
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- UniProt
- Q7P0X5
- Pockets
- 2 · best druggability 0.80
Structure
1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase | protein | 417 | 33% helix, 27% strand | Q7P0X5 |
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 | 556 | 0.80 | 0.86 | 54 | empty |
| 2 | 63 | 0.37 | 0.79 | 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 Q7P0X5
- Elsewhere: UniProt Q7P0X5 · AlphaFold DB Q7P0X5
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