Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q5GSC8)
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
- Q5GSC8
- Type
- protein
- Length
- 498 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9083d02dD1150e409871618C7e012e864fA13fe4
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- Q5GSC8
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 498 | 41% helix, 20% strand | Q5GSC8 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 971 | 0.73 | 0.77 | 88 | empty |
| 2 | 325 | 0.60 | 0.78 | 35 | empty |
| 3 | 90 | 0.52 | 0.83 | 18 | empty |
| 4 | 112 | 0.37 | 0.74 | 19 | empty |
| 5 | 50 | 0.36 | 0.80 | 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 Q5GSC8
- Elsewhere: UniProt Q5GSC8 · AlphaFold DB Q5GSC8
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