Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (B2J5G4)
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
- B2J5G4
- Type
- protein
- Length
- 363 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xFA658c241899DD6080b98c8D8783B12085F2a9A6
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- B2J5G4
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 363 | 69% helix, 2% strand | B2J5G4 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 600 | 0.72 | 0.80 | 55 | empty |
| 2 | 143 | 0.49 | 0.78 | 22 | empty |
| 3 | 91 | 0.39 | 0.76 | 19 | empty |
| 4 | 53 | 0.29 | 0.75 | 15 | empty |
| 5 | 62 | 0.29 | 0.74 | 15 | 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 B2J5G4
- Elsewhere: UniProt B2J5G4 · AlphaFold DB B2J5G4
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