› 1k3d

X-ray diffraction
2Å resolution

Phosphoenolpyruvate carboxykinase in complex with ADP and AlF3

Released:
DOI: 10.2210/pdb1k3d/pdb
PDB entry 1k3d coloured by chain, front view.
PDB entry 1k3d coloured by chain, side view.
PDB entry 1k3d coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3).
Sudom AM, Prasad L, Goldie H, Delbaere LT
J Mol Biol 314 83-92 (2001)
PMID: 11724534

Function and Biology Details

Reaction catalysed: 
ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149561 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxykinase (ATP) Chain: A
Molecule details ›
Chain: A
Length: 540 amino acids
Theoretical weight: 59.71 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P22259 (Residues: 1-540; Coverage: 100%)
Gene names: JW3366, b3403, pck, pckA
Sequence domains: Phosphoenolpyruvate carboxykinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand ADP 1 x ADP
Ligand AF3 1 x AF3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: C2
Unit cell:
a: 126.033Å b: 95.844Å c: 46.608Å
α: 90° β: 95.59° γ: 90°
R-values:
R R work R free
0.198 0.196 0.266
Expression system: Escherichia coli K-12

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Citations

1 review citation

Structural insights into the mechanism of phosphoenolpyruvate carboxykinase catalysis.
Carlson et al. (2009)
18 other articles

1 mention without citation

Massively parallel functional photoacoustic computed tomography of the human brain.
Na et al. (2022)