MolNFT v1 · #250213 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (Q1CE02)
Q1CE02: “AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (Q1CE02)”. 2 pockets (best druggability 0.80). MolNFT v1 #250213 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q1CE02
- Type
- protein
- Length
- 420 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE62cf5f8099Ce84aA2995668D94FA4133Ce9BFAa
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- UniProt
- Q1CE02
- Pockets
- 2 · best druggability 0.80
Structure
1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase | protein | 420 | 34% helix, 28% strand | Q1CE02 |
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 | 558 | 0.80 | 0.86 | 51 | empty |
| 2 | 75 | 0.36 | 0.77 | 18 | 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 Q1CE02
- Elsewhere: UniProt Q1CE02 · AlphaFold DB Q1CE02
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