Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (B1WV74)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (B1WV74) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1WV74
- Type
- protein
- Length
- 535 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x26d701FD7CF8553Cf8118D286dEca6D9740dA639
- Molecule
- CTP synthase
- UniProt
- B1WV74
- Pockets
- 5 · best druggability 0.64
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 535 | 43% helix, 22% strand | B1WV74 |
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 | 125 | 0.64 | 0.87 | 24 | empty |
| 2 | 386 | 0.58 | 0.75 | 50 | empty |
| 3 | 84 | 0.41 | 0.79 | 16 | empty |
| 4 | 62 | 0.35 | 0.78 | 16 | empty |
| 5 | 75 | 0.32 | 0.74 | 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 B1WV74
- Elsewhere: UniProt B1WV74 · AlphaFold DB B1WV74
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