Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (A1US92)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (A1US92) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1US92
- Type
- protein
- Length
- 542 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x46EfCa788d03A3e879DAcDb96552AB8Bbc7e20b3
- Molecule
- CTP synthase
- UniProt
- A1US92
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 542 | 40% helix, 22% strand | A1US92 |
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 | 214 | 0.70 | 0.87 | 33 | empty |
| 2 | 513 | 0.63 | 0.76 | 58 | empty |
| 3 | 131 | 0.41 | 0.75 | 25 | empty |
| 4 | 92 | 0.35 | 0.75 | 20 | empty |
| 5 | 63 | 0.33 | 0.76 | 10 | 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 A1US92
- Elsewhere: UniProt A1US92 · AlphaFold DB A1US92
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