› 3uqd

X-ray diffraction
2.14Å resolution

Crystal structure of the Phosphofructokinase-2 from Escherichia coli in complex with substrates and products

Released:
DOI: 10.2210/pdb3uqd/pdb
PDB entry 3uqd coloured by chain, front view.
PDB entry 3uqd coloured by chain, side view.
PDB entry 3uqd coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Studying the phosphoryl transfer mechanism of the E. coli phosphofructokinase-2: from X-ray structure to quantum mechanics/molecular mechanics simulations.
Murillo-López J, Zinovjev K, Pereira H, Caniuguir A, Garratt R, Babul J, Recabarren R, Alzate-Morales J, Caballero J, Tuñón I, Cabrera R
Chem Sci 10 2882-2892 (2019)
PMID: 30996866

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, C, D
Molecule details ›
Chains: A, B, C, D
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

5 bound ligands:
Ligand ATP 4 x ATP
Ligand F6P 2 x F6P
Ligand MG 6 x MG
Ligand FBP 2 x FBP
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: C2221
Unit cell:
a: 69.885Å b: 155.189Å c: 224.989Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.195 0.255
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 citation in other articles

Molecular Basis of Sulfosugar Selectivity in Sulfoglycolysis.
Sharma et al. (2021)
5 more

3 mentions without citation

Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation.
Kuhn et al. (2014)
2 more