Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q7VQH4)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q7VQH4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7VQH4
- Type
- protein
- Length
- 550 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- CTP synthase
- UniProt
- Q7VQH4
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 550 | 41% helix, 22% strand | Q7VQH4 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.73 | 0.91 | 32 | empty |
| 2 | 199 | 0.48 | 0.75 | 24 | empty |
| 3 | 190 | 0.46 | 0.75 | 29 | empty |
| 4 | 64 | 0.40 | 0.80 | 13 | empty |
| 5 | 86 | 0.32 | 0.73 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q7VQH4
- Elsewhere: UniProt Q7VQH4 · AlphaFold DB Q7VQH4
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