IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Tissue-specific structure/function differentiation of the liver isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. Tissue-specific structure/function differentiation of the liver isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. J. Biol. Chem. (0021-9258) 2003 Lee YH., Li Y., Uyeda K., Hasemann CA. leeyon@missouri.edu in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Lee YH., Li Y., Uyeda K., Hasemann CA. leeyon@missouri.edu Annotation to indicate that this entry has been checked and accepted by a senior curator. J. Biol. Chem. (0021-9258) 2003 f261_human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 6PF-2-K/Fru-2,6-P2ase liver isozyme PFKFB1 F6PK PFRX protein protein human Homo sapiens Human MSPEMGELTQTRLQKIWIPHSSGSSRLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSYKNYEFFLPDNMEALQIRKQCALAALKDVHNYLSHEEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREKVLEDFLKRIECYEVNYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHIQSRTVYYLMNIHVTPRSIYLCRHGESELNIRGRIGGDSGLSVRGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALGVPYEQWKALNEIDAGVCEEMTYEEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVLVICHQAVMRCLLAYFLDKSSDELPYLKCPLHTVLKLTPVAYGCKVESIYLNVEAVNTHREKPENVDITREPEEALDTVPAHY C4FF081A295FB7D3 pfkfb1-1 1 2 unspecified role unspecified role neutral component neutral component region binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain glu209 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 2 unspecified role unspecified role neutral component neutral component region binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain arg226 binding region binding-associated region binding region x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 9 6 direct interaction direct interaction working 21.7%, free 25.7% 2.40� A head-to-head homodimer of 432 amino acid residues per monomer (residues 39-470). Each subunit contains an ATPS, ADP, or Pi molecule bound to the kinase domain, and two inorganic phosphates bound to the bisphosphatase domain. No electron density is interpretable for the N-terminal regulatory fragment of residues 1-38, in which the phosphorylation site Ser-32 is located. The W0 mutant form of the enzyme (all Trp residues and Pro2 mutated to Phe and Arg, respectively) was employed for this study because it has better expression in Escherichia coli with the same kinetic properties as the wild type