Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (A7HXX9)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (A7HXX9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7HXX9
- Type
- protein
- Length
- 542 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEfBeEE7915c401dDa9e52C7608ad40797D558f83
- Molecule
- CTP synthase
- UniProt
- A7HXX9
- Pockets
- 8 · best druggability 0.71
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 542 | 41% helix, 23% strand | A7HXX9 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.71 | 0.88 | 28 | empty |
| 2 | 307 | 0.54 | 0.75 | 38 | empty |
| 3 | 178 | 0.50 | 0.77 | 35 | empty |
| 4 | 182 | 0.46 | 0.75 | 24 | empty |
| 5 | 80 | 0.36 | 0.76 | 17 | 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 A7HXX9
- Elsewhere: UniProt A7HXX9 · AlphaFold DB A7HXX9
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