4I7E: 6-phosphofructokinase

Crystal Structure of the Bacillus stearothermophilus Phosphofructokinase Mutant D12A in Complex with PEP. Determined by X-ray diffraction at 2.0 Å resolution. Released 31 Jul 2013.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Bacillus stearothermophilus
Chains
4
Atoms
10,197
Mol. weight
137.17 kDa
Ligands
PEP
Released
31 Jul 2013

Explore 4I7E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4I7E contains 64 α-helices and 52 β-strands across 4 chains. 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: 16 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand3-971
α-helix16-2914
β-strand33-3751
α-helix40-467
β-strand49-5241
α-helix54-574
α-helix74-774
α-helix81-9111
β-strand97-10151
α-helix103-11412
β-strand119-12351
β-strand124-12522
β-strand137-13822
α-helix139-15315
β-strand161-16883
α-helix175-1839
β-strand188-19033
α-helix198-21013
β-strand216-22163
α-helix227-23812
β-strand241-24663
α-helix248-2525
α-helix255-2573
α-helix258-27720
β-strand282-28761
β-strand290-29561
α-helix296-3005
α-helix303-3042
α-helix308-31710
Chain B: 16 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand3-864
α-helix16-2914
β-strand33-3754
α-helix40-467
β-strand49-5134
α-helix54-574
α-helix74-774
α-helix79-9113
β-strand96-10164
α-helix103-11412
β-strand119-12354
β-strand12415
β-strand13715
α-helix139-15416
β-strand163-16866
α-helix175-18410
β-strand188-19036
α-helix198-21013
β-strand216-22166
α-helix227-23812
β-strand242-24656
α-helix248-2525
α-helix255-2573
α-helix258-27619
β-strand282-28764
β-strand290-29564
α-helix296-3016
α-helix303-3042
α-helix308-31710
Chain C: 16 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand3-867
α-helix16-2914
β-strand33-3757
α-helix40-467
β-strand49-5137
α-helix54-574
α-helix74-774
α-helix79-9113
β-strand97-10157
α-helix103-11412
β-strand119-12357
β-strand124-12528
β-strand137-13828
α-helix139-15315
β-strand163-16866
α-helix175-1839
β-strand188-19036
α-helix198-21114
β-strand216-22166
α-helix227-23812
β-strand242-24656
α-helix248-2525
α-helix255-2573
α-helix258-27619
β-strand282-28767
β-strand290-29567
α-helix296-3005
α-helix303-3042
α-helix308-31710
Chain D: 16 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand3-869
α-helix16-2914
β-strand33-3759
α-helix40-467
β-strand49-5249
α-helix54-574
α-helix74-774
α-helix79-9113
β-strand96-10169
α-helix103-11412
β-strand119-12359
β-strand124-125210
β-strand137-138210
α-helix139-15416
β-strand163-16863
α-helix175-18410
β-strand188-19033
α-helix198-21114
β-strand216-22163
α-helix227-23812
β-strand242-24653
α-helix248-2525
α-helix255-2573
α-helix258-27619
β-strand282-28769
β-strand290-29569
α-helix296-3005
α-helix303-3042
α-helix308-31710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
6-phosphofructokinaseA, B, C, Dprotein319Bacillus stearothermophilusP00512 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4I7E_1 6-phosphofructokinase (chains A, B, C, D)
MKRIGVLTSGGASPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDI
IHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCV
GVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWS
GLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGF
ETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL
ANKHTIDQRMYALSKELSI

Ligands and cofactors

IDNameFormulaCopies
PEPPhosphoenolpyruvateC3 H5 O6 P4

Primary citation

Redefining the Role of the Quaternary Shift in Bacillus stearothermophilus Phosphofructokinase. Mosser, R., Reddy, M.C., Bruning, J.B. et al. Biochemistry (2013) 52:5421-5429. DOI 10.1021/bi4002503 · 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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