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/ http://www.ebi.ac.uk/ kim-2006-1 Crystal structure of the hypoxia-inducible form of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3): a possible new target for cancer therapy. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Kim SG., Manes NP., El-Maghrabi MR., Lee YH. Cancer - Interactions investigated in the context of cancer His-tagged protein was purified, the tag was removed by thrombin treatment prior to crystallisation. The final purification was performed using Mono Q anion exchange chromatography and the protein maintained under reducing conditions. yhlee@lsu.edu J. Biol. Chem. (0021-9258) 2006 f263_human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 6PF-2-K/Fru-2,6-P2ase brain/placenta-type isozyme iPFK-2 Renal carcinoma antigen NY-REN-56 PFKFB3 protein protein human Homo sapiens Human MPLELTQSRVQKIWVPVDHRPSLPRSCGPKLTNSPTVIVMVGLPARGKTYISKKLTRYLNWIGVPTKVFNVGEYRREAVKQYSSYNFFRPDNEEAMKVRKQCALAALRDVKSYLAKEGGQIAVFDATNTTRERRHMILHFAKENDFKAFFIESVCDDPTVVASNIMEVKISSPDYKDCNSAEAMDDFMKRISCYEASYQPLDPDKCDRDLSLIKVIDVGRRFLVNRVQDHIQSRIVYYLMNIHVQPRTIYLCRHGENEHNLQGRIGGDSGLSSRGKKFASALSKFVEEQNLKDLRVWTSQLKSTIQTAEALRLPYEQWKALNEIDAGVCEELTYEEIRDTYPEEYALREQDKYYYRYPTGESYQDLVQRLEPVIMELERQENVLVICHQAVLRCLLAYFLDKSAEEMPYLKCPLHTVLKLTPVAYGCRVESIYLNVESVCTHRERSEDAKKGPNPLMRRNSVTPLASPEPTKKPRINSFEEHVASTSAALPSCLPPEVPTQLPGQNMKGSRSSADSSRKH pfkfb3-pfkfbp3-1 Homodimerization of 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 by X-ray crystallography 256562 N/A 256563 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false 2.1A Head-to-head functional dimerization. The beta-hairpin N-terminus interacts with the 2-Pase domain to secure binding of fructose-6-phosphate to the active pocket Crystal also contains ATP, EDTA and fructose -6-phosphate