Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (B2I9M4)
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
- B2I9M4
- Type
- protein
- Length
- 425 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x35cE46a4a30196447966Bd34E1e090Eb6D1bAd3f
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- UniProt
- B2I9M4
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase | protein | 425 | 34% helix, 29% strand | B2I9M4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 525 | 0.78 | 0.85 | 55 | empty |
| 2 | 175 | 0.50 | 0.78 | 21 | empty |
| 3 | 89 | 0.36 | 0.75 | 18 | empty |
| 4 | 53 | 0.27 | 0.74 | 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 B2I9M4
- Elsewhere: UniProt B2I9M4 · AlphaFold DB B2I9M4
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