Research workbench
AlphaFold monomer V2.0 prediction for udp-N-acetylmuramoylalanine-- D-glutamate ligase (Q92I60)
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
- Q92I60
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf81d28bD872368aF456B77A1daFfa99d2d49F26C
- Molecule
- Udp-N-acetylmuramoylalanine--D-glutamate ligase
- UniProt
- Q92I60
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramoylalanine--D-glutamate ligase | protein | 500 | 36% helix, 19% strand | Q92I60 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 715 | 0.71 | 0.78 | 83 | empty |
| 2 | 226 | 0.46 | 0.73 | 18 | empty |
| 3 | 106 | 0.43 | 0.78 | 19 | empty |
| 4 | 51 | 0.24 | 0.72 | 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 Q92I60
- Elsewhere: UniProt Q92I60 · AlphaFold DB Q92I60
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