Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (A1KUX8)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (A1KUX8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1KUX8
- Type
- protein
- Length
- 544 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x723ec01D8D0DEca6E929c34b24C0D4fFE2fA25ae
- Molecule
- CTP synthase
- UniProt
- A1KUX8
- Pockets
- 6 · best druggability 0.69
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 544 | 41% helix, 23% strand | A1KUX8 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 229 | 0.69 | 0.86 | 39 | empty |
| 2 | 300 | 0.56 | 0.76 | 36 | empty |
| 3 | 128 | 0.43 | 0.77 | 30 | empty |
| 4 | 90 | 0.40 | 0.77 | 19 | empty |
| 5 | 67 | 0.38 | 0.79 | 16 | 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 A1KUX8
- Elsewhere: UniProt A1KUX8 · AlphaFold DB A1KUX8
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