› 4xyj

X-ray diffraction
3.1Å resolution

Crystal structure of human phosphofructokinase-1 in complex with ATP and Mg, Northeast Structural Genomics Consortium Target HR9275

Released:
DOI: 10.2210/pdb4xyj/pdb
PDB entry 4xyj coloured by chain, front view.
PDB entry 4xyj coloured by chain, side view.
PDB entry 4xyj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations.
Webb BA, Forouhar F, Szu FE, Seetharaman J, Tong L, Barber DL
Nature 523 111-4 (2015)
PMID: 25985179

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-169633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent 6-phosphofructokinase, platelet type Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 812 amino acids
Theoretical weight: 89.14 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: Q01813 (Residues: 1-784; Coverage: 100%)
Gene names: PFKF, PFKP
Sequence domains: Phosphofructokinase

Ligands and Environments

4 bound ligands:
Ligand ATP 8 x ATP
Ligand MG 15 x MG
Ligand PO4 12 x PO4
Ligand CO 2 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21
Unit cell:
a: 137.199Å b: 159.329Å c: 170.533Å
α: 90° β: 104.2° γ: 90°
R-values:
R R work R free
0.221 0.221 0.246
Expression system: unidentified baculovirus

Quick links

Citations

13 review citations

Glycogen metabolism in humans.
Adeva-Andany et al. (2016)
12 more

6 mentions without citation

Regulation of Cellular Metabolism through Phase Separation of Enzymes.
Prouteau et al. (2018)
5 more