Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (A1KVL5)
Analyse AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1KVL5
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD08fc2CFCBB59D4F39094eb15372af9cE86A61f6
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- A1KVL5
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 445 | 36% helix, 22% strand | A1KVL5 |
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 | 382 | 0.66 | 0.80 | 43 | empty |
| 2 | 266 | 0.57 | 0.78 | 34 | empty |
| 3 | 93 | 0.43 | 0.79 | 20 | empty |
| 4 | 76 | 0.36 | 0.76 | 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 A1KVL5
- Elsewhere: UniProt A1KVL5 · AlphaFold DB A1KVL5
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