Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q13X05)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q13X05) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q13X05
- Type
- protein
- Length
- 557 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- CTP synthase
- UniProt
- Q13X05
- Pockets
- 6 · best druggability 0.67
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 557 | 41% helix, 23% strand | Q13X05 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.67 | 0.87 | 28 | empty |
| 2 | 318 | 0.57 | 0.76 | 37 | empty |
| 3 | 200 | 0.50 | 0.76 | 29 | empty |
| 4 | 69 | 0.35 | 0.77 | 14 | empty |
| 5 | 77 | 0.29 | 0.73 | 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 Q13X05
- Elsewhere: UniProt Q13X05 · AlphaFold DB Q13X05
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