Structure of PDB 1mto Chain E

Receptor sequence

>1mtoE (length=319) Species: 1422 (Geobacillus stearothermophilus)

MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIK
KLEVGDVGDIIHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVI
GGDGSYQGAKKLTEHGFPCVGVPGTIDNDIPGTDFTIGFDTALNTVIDAI
DKIRDTATSHERTWVIEVMGRHAGDIALYSGLAGGAETILIPEADYDMND
VIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGFETRVTVLGHV
QRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL
ANKHTIDQRMYALSKELSI

3D structure

• PDB: 1mto Reversible Ligand-Induced Dissociation of a Tryptophan-Shift Mutant of Phosphofructokinase from Bacillus stearothermophilus
• Chain: E
• Resolution: 3.2 Å

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	F6P	E	D127 M169 R171 E222 R252	D127 M169 R171 E222 R252
BS02	F6P	E	R162 R243	R162 R243

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

External links

• PDB: RCSB:1mto, PDBe:1mto, PDBj:1mto
• PDBsum: 1mto
• PubMed: 12390023
• UniProt: P00512|PFKA_GEOSE ATP-dependent 6-phosphofructokinase (Gene Name=pfkA)