Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (A4Y944)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (A4Y944) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4Y944
- Type
- protein
- Length
- 545 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- CTP synthase
- UniProt
- A4Y944
- Pockets
- 6 · best druggability 0.65
Structure
1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 545 | 43% helix, 23% strand | A4Y944 |
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 | 173 | 0.65 | 0.85 | 32 | empty |
| 2 | 230 | 0.52 | 0.76 | 35 | empty |
| 3 | 215 | 0.47 | 0.74 | 27 | empty |
| 4 | 126 | 0.41 | 0.75 | 22 | empty |
| 5 | 50 | 0.28 | 0.75 | 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 A4Y944
- Elsewhere: UniProt A4Y944 · AlphaFold DB A4Y944
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