› 1pfk

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS

Released:
DOI: 10.2210/pdb1pfk/pdb
PDB entry 1pfk coloured by chain, front view.
PDB entry 1pfk coloured by chain, side view.
PDB entry 1pfk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the complex of phosphofructokinase from Escherichia coli with its reaction products.
Shirakihara Y, Evans PR
J Mol Biol 204 973-94 (1988)
PMID: 2975709

Function and Biology Details

Reaction catalysed: 
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-bisphosphate
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-141566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase isozyme 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 34.89 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A796 (Residues: 1-320; Coverage: 100%)
Gene names: JW3887, b3916, pfkA
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand FBP 2 x FBP
Ligand MG 4 x MG
Ligand ADP 4 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 112.3Å b: 85.4Å c: 77.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 not available not available
Expression system: Not provided

Quick links

Citations

16 review citations

Mechanisms of cooperativity and allosteric regulation in proteins.
Perutz MF. (1989)
15 more

20 mentions without citation

Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase.
Zhang et al. (2001)
19 more