› 2pfk

X-ray diffraction
2.4Å resolution

THE CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb2pfk/pdb
PDB entry 2pfk coloured by chain, front view.
PDB entry 2pfk coloured by chain, side view.
PDB entry 2pfk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of unliganded phosphofructokinase from Escherichia coli.
Rypniewski WR, Evans PR
J Mol Biol 207 805-21 (1989)
PMID: 2527305

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141565 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase isozyme 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 320 amino acids
Theoretical weight: 34.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A796 (Residues: 1-320; Coverage: 100%)
Gene names: JW3887, b3916, pfkA
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 177Å b: 66.4Å c: 154Å
α: 90° β: 118.8° γ: 90°
R-values:
R R work R free
0.166 not available not available
Expression system: Escherichia coli

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Citations

1 review citation

Evolution of glycolysis.
Fothergill-Gilmore et al. (1993)
32 other articles

7 mentions without citation

A network representation of protein structures: implications for protein stability.
Brinda et al. (2005)
6 more