Structure of PDB 6pfk Chain D

Receptor sequence
>6pfkD (length=319) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIK
KLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVI
GGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAI
DKIRDTATSHERTYVIEVMGRHAGDIALWSGLAGGAETILIPEADYDMND
VIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHV
QRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL
ANKHTIDQRMYALSKELSI
3D structure
PDB6pfk Structural basis of the allosteric behaviour of phosphofructokinase.
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G11 R72 C73 D103 G104 G124 T125 D127 D129 R171
Catalytic site (residue number reindexed from 1) G11 R72 C73 D103 G104 G124 T125 D127 D129 R171
Enzyme Commision number 2.7.1.11: 6-phosphofructokinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 PGA D R21 R25 G58 R21 R25 G58
BS02 PGA D R154 R211 K213 K214 R154 R211 K213 K214
Gene Ontology
Molecular Function
GO:0003872 6-phosphofructokinase activity
GO:0005524 ATP binding
GO:0008443 phosphofructokinase activity
GO:0016208 AMP binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0048029 monosaccharide binding
GO:0070095 fructose-6-phosphate binding
Biological Process
GO:0006002 fructose 6-phosphate metabolic process
GO:0006096 glycolytic process
GO:0016310 phosphorylation
GO:0030388 fructose 1,6-bisphosphate metabolic process
GO:0061621 canonical glycolysis
Cellular Component
GO:0005737 cytoplasm
GO:0005945 6-phosphofructokinase complex

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Molecular Function

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Cellular Component
External links
PDB RCSB:6pfk, PDBe:6pfk, PDBj:6pfk
PDBsum6pfk
PubMed2136935
UniProtP00512|PFKA_GEOSE ATP-dependent 6-phosphofructokinase (Gene Name=pfkA)

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