Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q0AD92)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q0AD92) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0AD92
- Type
- protein
- Length
- 564 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- CTP synthase
- UniProt
- Q0AD92
- Pockets
- 5 · best druggability 0.67
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 564 | 41% helix, 22% strand | Q0AD92 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 135 | 0.67 | 0.88 | 26 | empty |
| 2 | 310 | 0.58 | 0.77 | 42 | empty |
| 3 | 224 | 0.52 | 0.76 | 34 | empty |
| 4 | 106 | 0.39 | 0.75 | 21 | empty |
| 5 | 61 | 0.32 | 0.76 | 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 Q0AD92
- Elsewhere: UniProt Q0AD92 · AlphaFold DB Q0AD92
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