DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure (London, England : 1993) 1997 imex curation Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnström K., Sjöberg BM., Eklund H. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnström K., Sjöberg BM., Eklund H. DIP original experiment: DIP-263250X Structure (London, England : 1993) 1997 IMEx Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. rir1_ecoli Ribonucleoside-diphosphate reductase 1 subunit alpha nrdA dnaF Protein B1 b2234 Ribonucleoside-diphosphate reductase 1 R1 subunit Ribonucleotide reductase 1 JW2228 protein protein ecoli Escherichia coli (strain K12) MNQNLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQYLAARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYLVQNRVTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINATSSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLKNNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDITLFSPSDVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFSLMMQERASTGRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVNDENGEIALCTLSAFNLGAINNLDELEELAILAVRALDALLDYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELAKEQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALRESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRGYVSIKASKDGILRQVVPDYEHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSRFPSGKVPMQQLLKDLLTAYKFGVKTLYYQNTRDGAEDAQDDLVPSIQDDGCESGACKI DIP protein P00452 original sequence version: 158 DIP protein P00452 original sequence version: 162 DIP protein P00452-1 original sequence version: 145 DIP protein P00452 original sequence version: 144 DIP protein P00452 original sequence version: null 7E034F154567C3FC rir2_ecoli Ribonucleoside-diphosphate reductase 1 subunit beta Ribonucleotide reductase 1 Protein B2 Protein R2 nrdB ftsB b2235 JW2229 protein protein ecoli Escherichia coli (strain K12) MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL DIP protein P69924 original sequence version: 98 DIP protein P69924 original sequence version: 103 DIP protein P69924 original sequence version: 84 DIP protein P69924 original sequence version: 83 BF2D9A49B643E84A nrda-nrdb-2 1 3 unspecified role unspecified role unspecified role unspecified role 357-376 binding site 357-376 binding site sufficient to bind sufficient binding region sufficient to bind predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 2 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction