MolNFT v1 · #250111 · protein
AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (Q5PLD1)
Q5PLD1: “AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase (Q5PLD1)”. 2 pockets (best druggability 0.81). MolNFT v1 #250111 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q5PLD1
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- UniProt
- Q5PLD1
- Pockets
- 2 · best druggability 0.81
Structure
1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase | protein | 419 | 35% helix, 27% strand | Q5PLD1 |
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 | 461 | 0.81 | 0.88 | 49 | empty |
| 2 | 51 | 0.36 | 0.79 | 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 Q5PLD1
- Elsewhere: UniProt Q5PLD1 · AlphaFold DB Q5PLD1
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