Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (Q7V9C3)
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
- Q7V9C3
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x45c0Ec32B09adb915b7685B3d9063C89E41866C1
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- Q7V9C3
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 488 | 38% helix, 22% strand | Q7V9C3 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 939 | 0.74 | 0.78 | 72 | empty |
| 2 | 418 | 0.69 | 0.81 | 54 | empty |
| 3 | 94 | 0.37 | 0.75 | 19 | empty |
| 4 | 62 | 0.34 | 0.77 | 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 Q7V9C3
- Elsewhere: UniProt Q7V9C3 · AlphaFold DB Q7V9C3
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