Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (B7IDI7)
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
- B7IDI7
- Type
- protein
- Length
- 415 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5C81F89466F453542F3C897d87cd887Ce1917b5e
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- UniProt
- B7IDI7
- Pockets
- 2 · best druggability 0.81
Structure
1 distinct chain · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase | protein | 415 | 35% helix, 28% strand | B7IDI7 |
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 | 517 | 0.81 | 0.87 | 56 | empty |
| 2 | 54 | 0.25 | 0.72 | 16 | 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 B7IDI7
- Elsewhere: UniProt B7IDI7 · AlphaFold DB B7IDI7
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