Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (A3NZL8)
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
- A3NZL8
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- A3NZL8
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 389 | 70% helix, 1% strand | A3NZL8 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.76 | 0.82 | 47 | empty |
| 2 | 168 | 0.52 | 0.78 | 27 | empty |
| 3 | 95 | 0.40 | 0.77 | 22 | empty |
| 4 | 68 | 0.26 | 0.72 | 18 | 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 A3NZL8
- Elsewhere: UniProt A3NZL8 · AlphaFold DB A3NZL8
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