Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (A0AKD7)
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
- A0AKD7
- Type
- protein
- Length
- 324 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcd38ee57516af74F8e67f1085a39c3741e4C0cda
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- A0AKD7
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 73% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 324 | 73% helix, 2% strand | A0AKD7 |
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 | 631 | 0.74 | 0.81 | 46 | empty |
| 2 | 53 | 0.30 | 0.75 | 13 | empty |
| 3 | 51 | 0.26 | 0.74 | 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 A0AKD7
- Elsewhere: UniProt A0AKD7 · AlphaFold DB A0AKD7
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