› 1fiy

X-ray diffraction
2.8Å resolution

THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM ESCHERICHIA COLI AT 2.8 A RESOLUTION

Released:
DOI: 10.2210/pdb1fiy/pdb
PDB entry 1fiy coloured by chain, front view.
PDB entry 1fiy coloured by chain, side view.
PDB entry 1fiy coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition.
Kai Y, Matsumura H, Inoue T, Terada K, Nagara Y, Yoshinaga T, Kihara A, Tsumura K, Izui K
Proc Natl Acad Sci U S A 96 823-8 (1999)
PMID: 9927652

Function and Biology Details

Reaction catalysed: 
Phosphate + oxaloacetate = H(2)O + phosphoenolpyruvate + HCO(3)(-)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133647 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxylase Chain: A
Molecule details ›
Chain: A
Length: 883 amino acids
Theoretical weight: 99.18 KDa
Source organism: Escherichia coli K-12
UniProt:
  • Canonical: P00864 (Residues: 1-883; Coverage: 100%)
Gene names: JW3928, b3956, glu, ppc
Sequence domains: Phosphoenolpyruvate carboxylase

Ligands and Environments

1 bound ligand:
Ligand ASP 1 x ASP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: I222
Unit cell:
a: 117.6Å b: 248.4Å c: 82.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 not available 0.259

Quick links

Citations

7 review citations

Ecological aspects of the distribution of different autotrophic CO2 fixation pathways.
Berg IA. (2011)
6 more

8 mentions without citation

Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition.
Kai et al. (1999)
7 more