Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (C1F461)
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
- C1F461
- Type
- protein
- Length
- 377 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- C1F461
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 71% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 377 | 71% helix, 1% strand | C1F461 |
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 | 732 | 0.73 | 0.79 | 47 | empty |
| 2 | 51 | 0.50 | 0.87 | 15 | empty |
| 3 | 93 | 0.43 | 0.78 | 25 | empty |
| 4 | 71 | 0.28 | 0.72 | 16 | 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 C1F461
- Elsewhere: UniProt C1F461 · AlphaFold DB C1F461
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