Research workbench
Crystal structure of the C-terminal catalytic domain of Plasmodium falciparum CTP:phosphocholine cytidylyltransferase with 4-(aminomethyl)pyridin-2-amine
Analyse Crystal structure of the C-terminal catalytic domain of Plasmodium falciparum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Q9W
- Type
- protein
- Length
- 133 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Plasmodium falciparum
- Molecule
- Cholinephosphate cytidylyltransferase
- EC
- 2.7.7.15
- UniProt
- Q8IEE9
- Ligands
- 9NN, GZ6
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · resolution 1.8 · 1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cholinephosphate cytidylyltransferase (EC 2.7.7.15) | protein | 133 | 35% helix, 21% strand | Q8IEE9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.62 | 0.78 | 38 | GZ6 |
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 Q8IEE9
- Elsewhere: RCSB PDB 7Q9W · PDBe 7Q9W · UniProt Q8IEE9
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