› 6k31

X-ray diffraction
2.6Å resolution

Crystal structure of pyrophosphate-dependent phosphoenolpyruvate carboxykinase (PPi-PEPCK)

Released:
DOI: 10.2210/pdb6k31/pdb
PDB entry 6k31 coloured by chain, front view.
PDB entry 6k31 coloured by chain, side view.
PDB entry 6k31 coloured by chain, top view.
Source organism: Actinomyces israelii
Primary publication:
Structural comparisons of phosphoenolpyruvate carboxykinases reveal the evolutionary trajectories of these phosphodiester energy conversion enzymes.
Chiba Y, Miyakawa T, Shimane Y, Takai K, Tanokura M, Nozaki T
J Biol Chem 294 19269-19278 (2019)
PMID: 31662435

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AiPEPCK Chains: A, B
Molecule details ›
Chains: A, B
Length: 1153 amino acids
Theoretical weight: 127 KDa
Source organism: Actinomyces israelii
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand CO 2 x CO
1 modified residue:
Ligand MSE 34 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P3221
Unit cell:
a: 160.439Å b: 160.439Å c: 200.16Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.241
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Emerging roles of cytosolic phosphoenolpyruvate kinase 1 (PCK1) in cancer.
Abate et al. (2023)
2 more

1 mention without citation

Structural comparisons of phosphoenolpyruvate carboxykinases reveal the evolutionary trajectories of these phosphodiester energy conversion enzymes.
Chiba et al. (2019)