Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (P28595)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (P28595) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P28595
- Type
- protein
- Length
- 544 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfD2aa30896c43ba48ACc736586610789048c2c7a
- Molecule
- CTP synthase
- UniProt
- P28595
- Pockets
- 6 · best druggability 0.69
Structure
1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 544 | 41% helix, 22% strand | P28595 |
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 | 142 | 0.69 | 0.89 | 25 | empty |
| 2 | 311 | 0.55 | 0.75 | 34 | empty |
| 3 | 166 | 0.46 | 0.75 | 22 | empty |
| 4 | 99 | 0.41 | 0.77 | 21 | empty |
| 5 | 66 | 0.33 | 0.76 | 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 P28595
- Elsewhere: UniProt P28595 · AlphaFold DB P28595
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