Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q0HZR5)
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
- Q0HZR5
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Bba4Dfcacaa163872Cb467D38Fc0e76d3D00cF3
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q0HZR5
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 488 | 38% helix, 24% strand | Q0HZR5 |
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 | 844 | 0.75 | 0.79 | 82 | empty |
| 2 | 64 | 0.36 | 0.78 | 15 | empty |
| 3 | 63 | 0.35 | 0.78 | 14 | empty |
| 4 | 74 | 0.34 | 0.76 | 13 | 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 Q0HZR5
- Elsewhere: UniProt Q0HZR5 · AlphaFold DB Q0HZR5
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