4I4I: 6-phosphofructokinase

Crystal Structure of Bacillus stearothermophilus Phosphofructokinase mutant T156A bound to PEP. Determined by X-ray diffraction at 2.49 Å resolution. Released 31 Jul 2013.

Method
X-ray diffraction
Resolution
2.49 Å
Organism
Geobacillus stearothermophilus
Chains
4
Atoms
9,741
Mol. weight
137.22 kDa
Ligands
PEP
Released
31 Jul 2013

Explore 4I4I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4I4I 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: 15 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand3-971
α-helix16-2914
β-strand33-3751
α-helix40-456
β-strand49-5131
α-helix74-774
α-helix79-9214
β-strand96-10161
α-helix103-11412
β-strand119-12351
β-strand124-12522
β-strand137-13822
α-helix139-15618
β-strand163-16863
α-helix175-18410
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-helix303-3042
α-helix308-31710
Chain B: 17 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand3-974
α-helix16-2914
β-strand33-3754
α-helix40-456
β-strand49-5244
α-helix531
α-helix54-574
α-helix74-774
α-helix79-9113
β-strand96-10164
α-helix105-11410
β-strand119-12354
β-strand124-12525
β-strand137-13825
α-helix139-15618
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-helix296-3005
α-helix303-3042
α-helix308-31710
Chain C: 16 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand3-977
α-helix16-2914
β-strand33-3757
α-helix40-467
β-strand49-5137
α-helix54-574
α-helix75-773
α-helix79-9214
β-strand96-10167
α-helix103-11412
β-strand119-12357
β-strand12418
β-strand13718
α-helix139-15618
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-helix258-27720
β-strand282-28767
β-strand290-29567
α-helix296-3016
α-helix303-3042
α-helix308-31710
Chain D: 16 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand3-979
α-helix16-2914
β-strand33-3759
α-helix40-456
β-strand49-5139
α-helix54-574
α-helix75-773
α-helix79-9113
β-strand96-10169
α-helix103-11412
β-strand119-12359
β-strand124-125210
β-strand137-138210
α-helix139-15618
β-strand163-16863
α-helix175-18410
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-strand282-28769
β-strand290-29569
α-helix296-3005
α-helix303-3042
α-helix308-31710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
6-phosphofructokinaseA, B, C, Dprotein319Geobacillus stearothermophilusP00512 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4I4I_1 6-phosphofructokinase (chains A, B, C, D)
MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDI
IHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCV
GVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDAATSHERTYVIEVMGRHAGDIALWS
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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