Research workbench
AlphaFold monomer V2.0 prediction for glutamate--cysteine ligase (Q0VSY7)
Analyse AlphaFold monomer V2.0 prediction for glutamate--cysteine ligase (Q0VSY7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0VSY7
- Type
- protein
- Length
- 525 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Glutamate--cysteine ligase
- UniProt
- Q0VSY7
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate--cysteine ligase | protein | 525 | 51% helix, 14% strand | Q0VSY7 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 853 | 0.77 | 0.81 | 78 | empty |
| 2 | 197 | 0.64 | 0.84 | 28 | empty |
| 3 | 64 | 0.30 | 0.74 | 15 | 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 Q0VSY7
- Elsewhere: UniProt Q0VSY7 · AlphaFold DB Q0VSY7
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