Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramate--L-alanine ligase (A0JV95)
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
- A0JV95
- Type
- protein
- Length
- 467 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcAef3C9C92b17a39121e7c4f847C9d185A4A2A15
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- UniProt
- A0JV95
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase | protein | 467 | 38% helix, 21% strand | A0JV95 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 478 | 0.67 | 0.79 | 59 | empty |
| 2 | 247 | 0.64 | 0.82 | 39 | empty |
| 3 | 51 | 0.26 | 0.74 | 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 A0JV95
- Elsewhere: UniProt A0JV95 · AlphaFold DB A0JV95
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