Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (Q0VS05)
Analyse AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0VS05
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc17764AdED8c1b2dc79039e2AF3d99e39dE06624
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- Q0VS05
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 72% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 360 | 72% helix, 2% strand | Q0VS05 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 729 | 0.77 | 0.82 | 59 | empty |
| 2 | 103 | 0.46 | 0.79 | 16 | empty |
| 3 | 62 | 0.27 | 0.72 | 13 | 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 Q0VS05
- Elsewhere: UniProt Q0VS05 · AlphaFold DB Q0VS05
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