Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (Q8FNT7)
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
- Q8FNT7
- Type
- protein
- Length
- 366 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8FaEF14B1a3E454aE2Cf5074731A50b14d68F3ac
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- Q8FNT7
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 366 | 69% helix, 4% strand | Q8FNT7 |
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 | 646 | 0.69 | 0.78 | 50 | empty |
| 2 | 116 | 0.42 | 0.77 | 26 | empty |
| 3 | 56 | 0.31 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q8FNT7
- Elsewhere: UniProt Q8FNT7 · AlphaFold DB Q8FNT7
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