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Crystal structure of the C-terminal catalytic domain of plasmodium falciparum CTP:PHOSPHOCHOLINE cytidylyltransferase in complex with phosphocholine

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
4ZCR
Type
protein
Length
128 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cholinephosphate cytidylyltransferase
EC
2.7.7.15
UniProt
Q8IEE9
Ligands
PC
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACholinephosphate cytidylyltransferase (EC 2.7.7.15)protein12838% helix, 22% strandQ8IEE9

Ligands and binding sites

  • PC · Phosphocholine · ligand · chains A

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13000.590.7836PC

Compared structures

  • 4ZCR · Crystal structure of the C-terminal catalytic domain of Plasmodium falciparum… · the same entry in another collection · chain A against A, TM-score 1.00

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