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/ takusagawa-1996-1 Structure and function of S-adenosylmethionine synthetase: crystal structures of S-adenosylmethionine synthetase with ADP, BrADP, and PPi at 28 angstroms resolution. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Takusagawa F., Kamitori S., Markham GD. Biochemistry (0006-2960) 1996 Only protein-protein interactions imex curation metk_ecoli S-adenosylmethionine synthase metK metX b2942 Methionine adenosyltransferase MAT JW2909 protein protein ecoli Escherichia coli (strain K12) MAKHLFTSESVSEGHPDKIADQISDAVLDAILEQDPKARVACETYVKTGMVLVGGEITTSAWVDIEEITRNTVREIGYVHSDMGFDANSCAVLSAIGKQSPDINQGVDRADPLEQGAGDQGLMFGYATNETDVLMPAPITYAHRLVQRQAEVRKNGTLPWLRPDAKSQVTFQYDDGKIVGIDAVVLSTQHSEEIDQKSLQEAVMEEIIKPILPAEWLTSATKFFINPTGRFVIGGPMGDCGLTGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAARYVAKNIVAAGLADRCEIQVSYAIGVAEPTSIMVETFGTEKVPSEQLTLLVREFFDLRPYGLIQMLDLLHPIYKETAAYGHFGREHFPWEKTDKAQLLRDAAGLK 97FA8CF17B542941 metk-metk-1 Crystal structure of S-adenosylmethionine synthetase 511262 N/A 511263 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) Stoichiometry: 4.0 direct interaction direct interaction false false false MAT consists of four identical subunits. Pairs of subunits (A and B or C and D) strongly interact with each other to form a spherical tight dimer, and these tight dimers associate to a peanut-shaped tetrameric enzyme. The interactions between the tight dimers appear to be much weaker than the subunit-subunit interactions within the tight dimer. Each tight dimer has two active sites located between subunits A and B or C and D, with amino acid residues from both subunits contributing to each active site. 2.80� working 19.0%, free 25.7%