› 1k3c

X-ray diffraction
2Å resolution

Phosphoenolpyruvate carboxykinase in complex with ADP, AlF3 and Pyruvate

Released:
DOI: 10.2210/pdb1k3c/pdb
PDB entry 1k3c coloured by chain, front view.
PDB entry 1k3c coloured by chain, side view.
PDB entry 1k3c 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: C2
Unit cell:
a: 124.738Å b: 94.211Å c: 46.336Å
α: 90° β: 96.05° γ: 90°
R-values:
R R work R free
0.225 0.223 0.285
Expression system: Escherichia coli K-12

Quick links

Citations

1 review citation

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

1 mention without citation

NSiteMatch: Prediction of Binding Sites of Nucleotides by Identifying the Structure Similarity of Local Surface Patches.
Sun et al. (2017)