Research workbench
AlphaFold monomer V2.0 prediction for phospho-N-acetylmuramoyl- pentapeptide-transferase (B1LXZ8)
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
- B1LXZ8
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x091F6E03f377Dec8A4a0efEE4B822E023605Dc04
- Molecule
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- UniProt
- B1LXZ8
- Pockets
- 4 · best druggability 0.75
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 | B1LXZ8 |
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 | 532 | 0.75 | 0.83 | 40 | empty |
| 2 | 96 | 0.49 | 0.81 | 17 | empty |
| 3 | 61 | 0.28 | 0.73 | 13 | empty |
| 4 | 57 | 0.25 | 0.72 | 11 | 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 B1LXZ8
- Elsewhere: UniProt B1LXZ8 · AlphaFold DB B1LXZ8
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