Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (A0R018)
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
- A0R018
- Type
- protein
- Length
- 493 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- A0R018
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 493 | 39% helix, 22% strand | A0R018 |
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 | 599 | 0.74 | 0.81 | 75 | empty |
| 2 | 152 | 0.45 | 0.76 | 29 | empty |
| 3 | 58 | 0.31 | 0.76 | 12 | 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 A0R018
- Elsewhere: UniProt A0R018 · AlphaFold DB A0R018
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