› 4i4i

X-ray diffraction
2.49Å resolution

Crystal Structure of Bacillus stearothermophilus Phosphofructokinase mutant T156A bound to PEP

Released:
DOI: 10.2210/pdb4i4i/pdb
PDB entry 4i4i coloured by chain, front view.
PDB entry 4i4i coloured by chain, side view.
PDB entry 4i4i coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase.
Mosser R, Reddy MC, Bruning JB, Sacchettini JC, Reinhart GD
Biochemistry 52 5421-9 (2013)
PMID: 23859543

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-132577 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 319 amino acids
Theoretical weight: 34.14 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00512 (Residues: 1-319; Coverage: 100%)
Gene names: pfk, pfkA
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PEP 4 x PEP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 96.405Å b: 111.575Å c: 129.448Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.166 0.238
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations.
Webb et al. (2015)
2 more

1 mention without citation

Redefining the role of the quaternary shift in Bacillus stearothermophilus phosphofructokinase.
Mosser et al. (2013)