Research workbench
AlphaFold monomer V2.0 prediction for CTP synthase (A3PFH8)
Analyse AlphaFold monomer V2.0 prediction for CTP synthase (A3PFH8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3PFH8
- Type
- protein
- Length
- 536 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xAB584A85A9D45Ce11453E831d49C4cb335302E5F
- Molecule
- CTP synthase
- UniProt
- A3PFH8
- Pockets
- 5 · best druggability 0.74
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CTP synthase | protein | 536 | 43% helix, 22% strand | A3PFH8 |
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 | 151 | 0.74 | 0.92 | 32 | empty |
| 2 | 254 | 0.52 | 0.75 | 36 | empty |
| 3 | 114 | 0.39 | 0.75 | 18 | empty |
| 4 | 71 | 0.36 | 0.77 | 17 | empty |
| 5 | 71 | 0.35 | 0.77 | 21 | 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 A3PFH8
- Elsewhere: UniProt A3PFH8 · AlphaFold DB A3PFH8
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