Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (B8F3B3)
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
- B8F3B3
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa468e9aC7533c96f63F5B3a2d6A012D6915744dF
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- B8F3B3
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 360 | 72% helix, 1% strand | B8F3B3 |
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 | 659 | 0.76 | 0.82 | 49 | empty |
| 2 | 107 | 0.42 | 0.77 | 20 | empty |
| 3 | 62 | 0.40 | 0.80 | 18 | empty |
| 4 | 51 | 0.23 | 0.71 | 11 | 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 B8F3B3
- Elsewhere: UniProt B8F3B3 · AlphaFold DB B8F3B3
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