Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (Q9PDG4)
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
- Q9PDG4
- Type
- protein
- Length
- 425 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x42e9263576E7016E0736d3e3f93ddd6E85E0D2Bd
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- UniProt
- Q9PDG4
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 35% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase | protein | 425 | 35% helix, 29% strand | Q9PDG4 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.77 | 0.84 | 57 | empty |
| 2 | 102 | 0.37 | 0.75 | 19 | empty |
| 3 | 99 | 0.36 | 0.75 | 17 | empty |
| 4 | 80 | 0.33 | 0.74 | 17 | 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 Q9PDG4
- Elsewhere: UniProt Q9PDG4 · AlphaFold DB Q9PDG4
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