Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q9V1S2)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q9V1S2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9V1S2
- Type
- protein
- Length
- 537 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6D396355C80AA8138D89B633c4D5ac7C46A9cfE7
- Molecule
- CTP synthase
- UniProt
- Q9V1S2
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 537 | 44% helix, 21% strand | Q9V1S2 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.66 | 0.87 | 27 | empty |
| 2 | 351 | 0.58 | 0.76 | 49 | empty |
| 3 | 79 | 0.42 | 0.79 | 16 | empty |
| 4 | 118 | 0.38 | 0.74 | 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 Q9V1S2
- Elsewhere: UniProt Q9V1S2 · AlphaFold DB Q9V1S2
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