Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (Q8RDQ0)
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
- Q8RDQ0
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x463a972e031C685D1BD2C43E9dFA3Ed66670D0bc
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- Q8RDQ0
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 71% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 361 | 71% helix, 2% strand | Q8RDQ0 |
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 | 561 | 0.69 | 0.79 | 38 | empty |
| 2 | 96 | 0.44 | 0.79 | 18 | empty |
| 3 | 60 | 0.30 | 0.75 | 14 | 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 Q8RDQ0
- Elsewhere: UniProt Q8RDQ0 · AlphaFold DB Q8RDQ0
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