Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q0APT7)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q0APT7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0APT7
- Type
- protein
- Length
- 542 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71588E5F8E9a83dA03D5148D4320336d807CA6D0
- Molecule
- CTP synthase
- UniProt
- Q0APT7
- Pockets
- 7 · best druggability 0.70
Structure
1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 542 | 40% helix, 23% strand | Q0APT7 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.70 | 0.86 | 38 | empty |
| 2 | 338 | 0.56 | 0.75 | 33 | empty |
| 3 | 138 | 0.46 | 0.77 | 19 | empty |
| 4 | 66 | 0.34 | 0.77 | 16 | empty |
| 5 | 60 | 0.30 | 0.75 | 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 Q0APT7
- Elsewhere: UniProt Q0APT7 · AlphaFold DB Q0APT7
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