Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (Q1BHS2)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (Q1BHS2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1BHS2
- Type
- protein
- Length
- 552 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- CTP synthase
- UniProt
- Q1BHS2
- Pockets
- 5 · best druggability 0.67
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 552 | 41% helix, 23% strand | Q1BHS2 |
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 | 173 | 0.67 | 0.87 | 30 | empty |
| 2 | 312 | 0.57 | 0.76 | 40 | empty |
| 3 | 199 | 0.50 | 0.76 | 30 | empty |
| 4 | 57 | 0.30 | 0.75 | 12 | empty |
| 5 | 58 | 0.26 | 0.73 | 12 | 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 Q1BHS2
- Elsewhere: UniProt Q1BHS2 · AlphaFold DB Q1BHS2
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