Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase 2 (Q927U1)
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
- Q927U1
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x934953E3d9faD9B1cC752f4A28d5f4E6903eA0Ce
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase 2
- UniProt
- Q927U1
- Pockets
- 2 · best druggability 0.81
Structure
1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase 2 | protein | 423 | 34% helix, 28% strand | Q927U1 |
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 | 542 | 0.81 | 0.87 | 51 | empty |
| 2 | 98 | 0.38 | 0.76 | 19 | 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 Q927U1
- Elsewhere: UniProt Q927U1 · AlphaFold DB Q927U1
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