Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (A0LTM0)
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
- A0LTM0
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc2d018C3B68758051786C757a4402031fe683775
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- A0LTM0
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-N-acetylmuramoyl-pentapeptide-transferase | protein | 354 | 68% helix, 4% strand | A0LTM0 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 553 | 0.74 | 0.82 | 43 | empty |
| 2 | 111 | 0.48 | 0.79 | 16 | empty |
| 3 | 51 | 0.34 | 0.79 | 16 | empty |
| 4 | 78 | 0.32 | 0.74 | 20 | 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 A0LTM0
- Elsewhere: UniProt A0LTM0 · AlphaFold DB A0LTM0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.