Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (A6VQN6)
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
- A6VQN6
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x100609714B35e7372d137b552e2e7d843682FA31
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- A6VQN6
- Pockets
- 2 · best druggability 0.74
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 | A6VQN6 |
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 | 563 | 0.74 | 0.82 | 45 | empty |
| 2 | 93 | 0.39 | 0.76 | 19 | 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 A6VQN6
- Elsewhere: UniProt A6VQN6 · AlphaFold DB A6VQN6
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