MolNFT v1 · #250214 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (A4THI5)
A4THI5: “AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (A4THI5)”. 2 pockets (best druggability 0.82). MolNFT v1 #250214 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A4THI5
- Type
- protein
- Length
- 420 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x74fEc74F9BDfb03f9F20b143612c52e41f0f54C3
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- UniProt
- A4THI5
- Pockets
- 2 · best druggability 0.82
Structure
1 distinct chain · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase | protein | 420 | 35% helix, 28% strand | A4THI5 |
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 | 480 | 0.82 | 0.89 | 47 | empty |
| 2 | 85 | 0.38 | 0.77 | 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 A4THI5
- Elsewhere: UniProt A4THI5 · AlphaFold DB A4THI5
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