Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (B5XMA3)
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
- B5XMA3
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA40142fE4BDa34A12E7e506aD8115eEBb8b9eedb
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- B5XMA3
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 452 | 38% helix, 21% strand | B5XMA3 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 503 | 0.61 | 0.75 | 58 | empty |
| 2 | 207 | 0.47 | 0.74 | 28 | empty |
| 3 | 98 | 0.43 | 0.78 | 17 | 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 B5XMA3
- Elsewhere: UniProt B5XMA3 · AlphaFold DB B5XMA3
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