4PFK: Phosphofructokinase. Structure and control

Phosphofructokinase. Structure and control. Determined by X-ray diffraction at 2.4 Å resolution. Released 9 Jan 1989.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Geobacillus stearothermophilus
Chains
1
Atoms
2,534
Mol. weight
35.33 kDa
Ligands
F6P, MG, ADP
Released
9 Jan 1989

Explore 4PFK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PFK contains 14 α-helices and 13 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 14 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand3-971
α-helix16-2914
β-strand33-3751
α-helix40-456
β-strand49-5241
α-helix54-574
α-helix79-9214
β-strand96-10161
α-helix103-11412
β-strand119-12351
β-strand12412
β-strand13712
α-helix139-15921
β-strand163-16863
α-helix175-1839
β-strand188-19033
α-helix198-21013
β-strand216-22163
α-helix227-23812
β-strand242-24653
α-helix248-2525
α-helix255-2573
α-helix258-27619
β-strand282-28761
β-strand290-29561
α-helix296-2994
α-helix309-31810

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PhosphofructokinaseAprotein319Geobacillus stearothermophilusP00512 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4PFK_1 PHOSPHOFRUCTOKINASE (chains A)
MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDI
IHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIQGLVVIGGDGSYQGAKKLTEHGFPCV
GVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWS
GLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGF
ETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL
ANKHTIDQRMYALSKELSI

Ligands and cofactors

IDNameFormulaCopies
F6P6-O-phosphono-beta-D-fructofuranoseC6 H13 O9 P1
MGMagnesium ionMg2
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P22

Primary citation

Phosphofructokinase: structure and control. Evans, P.R., Farrants, G.W., Hudson, P.J. Philos Trans R Soc London,ser B (1981) 293:53-62. PubMed

Other PDB entries of the same protein (UniProt P00512 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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