UniProt UniProt http://www.uniprot.org wu-2007c-1 Structure and mechanism of spermidine synthases. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Wu H., Min J., Ikeguchi Y., Zeng H., Dong A., Loppnau P., Pegg A.E., Plotnikov A.N. alexander.plotnikov@utoronto.ca Biochemistry (0006-2960) 2007 Only protein-protein interactions imex curation spee_human Spermidine synthase SRM SPS1 SRML1 Putrescine aminopropyltransferase protein protein human Homo sapiens Human MEPGPDGPAASGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPTYPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALNDVS spee-1 1166915 n/a 1166916 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecoli Escherichia coli (strain K12) Stoichiometry: 2.0 direct interaction direct interaction false false false R-value 0.179 R free 0.228 1.89 A group deposited 4 structures for this protein, (2O05, 2O06, 2O07, 2O0L), showed R-factors and resolution for the one with the highest resolution =2O07