Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (B4E6J5)
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
- B4E6J5
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd9e069D1339FAA95b9530BA8d5279541BF7Eeaab
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- B4E6J5
- Pockets
- 2 · best druggability 0.76
Structure
1 distinct chain · 71% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 389 | 71% helix, 2% strand | B4E6J5 |
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 | 754 | 0.76 | 0.81 | 71 | empty |
| 2 | 85 | 0.39 | 0.77 | 25 | 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 B4E6J5
- Elsewhere: UniProt B4E6J5 · AlphaFold DB B4E6J5
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