Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (A5N7E7)
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
- A5N7E7
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x50F056e931C4086d123dE7fb8d7aBA0dfD1BE17B
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- A5N7E7
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 72% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 317 | 72% helix, 3% strand | A5N7E7 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 616 | 0.72 | 0.80 | 48 | empty |
| 2 | 91 | 0.42 | 0.78 | 19 | empty |
| 3 | 65 | 0.31 | 0.74 | 15 | empty |
| 4 | 52 | 0.26 | 0.73 | 10 | 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 A5N7E7
- Elsewhere: UniProt A5N7E7 · AlphaFold DB A5N7E7
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