Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (B0US64)
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
- B0US64
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x81Cb9D6826c494c4199378382c6Eb30Ba05CC2C7
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- B0US64
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 71% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 361 | 71% helix, 1% strand | B0US64 |
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 | 620 | 0.77 | 0.83 | 45 | empty |
| 2 | 98 | 0.41 | 0.77 | 16 | empty |
| 3 | 54 | 0.32 | 0.76 | 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 B0US64
- Elsewhere: UniProt B0US64 · AlphaFold DB B0US64
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