Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q0BXU4)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0BXU4
- Type
- protein
- Length
- 474 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA15011e6fCb04bD3567F1C0feB9323b96C9D1706
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q0BXU4
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 474 | 36% helix, 24% strand | Q0BXU4 |
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 | 700 | 0.71 | 0.78 | 90 | empty |
| 2 | 82 | 0.39 | 0.78 | 24 | empty |
| 3 | 83 | 0.38 | 0.76 | 17 | 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 Q0BXU4
- Elsewhere: UniProt Q0BXU4 · AlphaFold DB Q0BXU4
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