› 4off

X-ray diffraction
1.89Å resolution

Crystal structure of apo carboxy cGMP binding domain of Plasmodium falciparum PKG

Released:
DOI: 10.2210/pdb4off/pdb
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PDB entry 4off coloured by chain, front view.
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PDB entry 4off coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Crystal structures of the carboxyl cGMP binding domain of the Plasmodium falciparum cGMP-dependent protein kinase reveal a novel capping triad crucial for merozoite egress.
Kim JJ, Flueck C, Franz E, Sanabria-Figueroa E, Thompson E, Lorenz R, Bertinetti D, Baker DA, Herberg FW, Kim C
OpenAccess logo PLoS Pathog 11 e1004639 (2015)
PMID: 25646845

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cGMP-dependent protein kinase Chain: A
Molecule details ›
Chain: A
Length: 144 amino acids
Theoretical weight: 16.95 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8I719 (Residues: 401-542; Coverage: 17%)
Gene names: PF3D7_1436600, PKG
Sequence domains: Cyclic nucleotide-binding domain

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P212121
Unit cell:
a: 25.781Å b: 57.683Å c: 82.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.228
Expression system: Escherichia coli

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Citations

6 review citations

cGMP: a unique 2nd messenger molecule - recent developments in cGMP research and development.
Friebe et al. (2020)
5 more

4 mentions without citation

Crystal structures of the carboxyl cGMP binding domain of the Plasmodium falciparum cGMP-dependent protein kinase reveal a novel capping triad crucial for merozoite egress.
Kim et al. (2015)
3 more

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