› 3o8n

X-ray diffraction
3.2Å resolution

Structure of phosphofructokinase from rabbit skeletal muscle

Released:
DOI: 10.2210/pdb3o8n/pdb
PDB entry 3o8n coloured by chain, front view.
PDB entry 3o8n coloured by chain, side view.
PDB entry 3o8n coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle.
Banaszak K, Mechin I, Obmolova G, Oldham M, Chang SH, Ruiz T, Radermacher M, Kopperschläger G, Rypniewski W
J Mol Biol 407 284-97 (2011)
PMID: 21241708

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase, muscle type Chains: A, B
Molecule details ›
Chains: A, B
Length: 762 amino acids
Theoretical weight: 83.27 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00511 (Residues: 1-762; Coverage: 98%)
Gene name: PFKM
Sequence domains: Phosphofructokinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ADP 6 x ADP
Ligand PO4 6 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P6122
Unit cell:
a: 163.292Å b: 163.292Å c: 356.939Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.302
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Dysregulated pH: a perfect storm for cancer progression.
Webb et al. (2011)
3 more

4 mentions without citation

Selective activation of PFKL suppresses the phagocytic oxidative burst.
Amara et al. (2021)
3 more