Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (B0V675)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (B0V675) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0V675
- Type
- protein
- Length
- 545 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8e1Ea8ACD4137C45Bd166cE0e156CFc7ab0b5783
- Molecule
- CTP synthase
- UniProt
- B0V675
- Pockets
- 5 · best druggability 0.66
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 545 | 41% helix, 23% strand | B0V675 |
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 | 240 | 0.66 | 0.83 | 40 | empty |
| 2 | 230 | 0.54 | 0.77 | 30 | empty |
| 3 | 223 | 0.49 | 0.75 | 27 | empty |
| 4 | 118 | 0.38 | 0.74 | 23 | empty |
| 5 | 114 | 0.37 | 0.74 | 25 | 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 B0V675
- Elsewhere: UniProt B0V675 · AlphaFold DB B0V675
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