› 1khg

X-ray diffraction
2.34Å resolution

Function and Biology Details

Reaction catalysed: 
GTP + oxaloacetate = GDP + 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-152943 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxykinase, cytosolic [GTP] Chain: A
Molecule details ›
Chain: A
Length: 625 amino acids
Theoretical weight: 69.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35558 (Residues: 1-622; Coverage: 100%)
Gene names: PCK1, PEPCK1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MN 1 x MN
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 45.388Å b: 60.872Å c: 61.974Å
α: 88.69° β: 70.13° γ: 72.37°
R-values:
R R work R free
0.19 0.185 0.281
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria.
Sauer et al. (2005)
5 more

4 mentions without citation

c.A2456C-substitution in Pck1 changes the enzyme kinetic and functional properties modifying fat distribution in pigs.
Latorre et al. (2016)
3 more