Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q927T4)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q927T4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q927T4
- Type
- protein
- Length
- 532 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- CTP synthase
- UniProt
- Q927T4
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 532 | 43% helix, 22% strand | Q927T4 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.73 | 0.96 | 18 | empty |
| 2 | 244 | 0.52 | 0.76 | 33 | empty |
| 3 | 77 | 0.48 | 0.83 | 19 | empty |
| 4 | 64 | 0.28 | 0.73 | 12 | empty |
| 5 | 50 | 0.25 | 0.73 | 15 | 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 Q927T4
- Elsewhere: UniProt Q927T4 · AlphaFold DB Q927T4
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