› 3cqd

X-ray diffraction
1.98Å resolution

Structure of the tetrameric inhibited form of phosphofructokinase-2 from Escherichia coli

Released:
DOI: 10.2210/pdb3cqd/pdb
PDB entry 3cqd coloured by chain, front view.
PDB entry 3cqd coloured by chain, side view.
PDB entry 3cqd coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition.
Cabrera R, Ambrosio AL, Garratt RC, Guixé V, Babul J
J Mol Biol 383 588-602 (2008)
PMID: 18762190

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase isozyme 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 32.49 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06999 (Residues: 1-309; Coverage: 100%)
Gene names: JW5280, b1723, pfkB
Sequence domains: pfkB family carbohydrate kinase
Structure domains: UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand ATP 4 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P2221
Unit cell:
a: 42.822Å b: 86.834Å c: 171.308Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.234
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Hydrogen-deuterium exchange mass spectrometry reveals folding and allostery in protein-protein interactions.
Ramirez-Sarmiento et al. (2018)
15 other articles

8 mentions without citation

ATPsite: sequence-based prediction of ATP-binding residues.
Chen et al. (2011)
7 more