Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q7VUQ4)
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
- Q7VUQ4
- Type
- protein
- Length
- 468 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q7VUQ4
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 468 | 37% helix, 26% strand | Q7VUQ4 |
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 | 581 | 0.73 | 0.81 | 64 | empty |
| 2 | 57 | 0.38 | 0.80 | 12 | empty |
| 3 | 78 | 0.37 | 0.77 | 13 | empty |
| 4 | 64 | 0.36 | 0.78 | 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 Q7VUQ4
- Elsewhere: UniProt Q7VUQ4 · AlphaFold DB Q7VUQ4
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