MolNFT v1 · #243215 · protein
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (A4VIH5)
A4VIH5 · Phospho-N-acetylmuramoyl-pentapeptide-transferase: “AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (A4VIH5)”. 2 pockets (best druggability 0.72). MolNFT v1 #243215 on GenesisL1: 3D…
- Accession
- A4VIH5
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- A4VIH5
- Pockets
- 2 · best druggability 0.72
Structure
1 distinct chain · 71% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 360 | 71% helix, 2% strand | A4VIH5 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 522 | 0.72 | 0.81 | 42 | empty |
| 2 | 126 | 0.51 | 0.80 | 21 | 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 A4VIH5
- Elsewhere: UniProt A4VIH5 · AlphaFold DB A4VIH5
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