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/ furusawa-2004-1 Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Furusawa Y., Nagarajan V., Tanokura M., Masai E., Fukuda M., Senda T. PDBe - Data obtained from the Protein Data Bank Europe J. Mol. Biol. (0022-2836) 2004 bpha1_rhojr Biphenyl 2,3-dioxygenase subunit alpha bphA1 bphAa RHA1_ro08060 Biphenyl dioxygenase system, oxygenase component subunit alpha Rieske dioxygenase Terminal oxygenase component of biphenyl dioxygenase, large subunit protein protein rhosr Rhodococcus sp. (strain RHA1) MTDVQCEPALAGRKPKWADADIAELVDERTGRLDPRIYTDEALYEQELERIFGRSWLLMGHETQIPKAGDFMTNYMGEDPVMVVRQKNGEIRVFLNQCRHRGMRICRADGGNAKSFTCSYHGWAYDTGGNLVSVPFEEQAFPGLRKEDWGPLQARVETYKGLIFANWDADAPDLDTYLGEAKFYMDHMLDRTEAGTEAIPGIQKWVIPCNWKFAAEQFCSDMYHAGTTSHLSGILAGLPDGVDLSELAPPTEGIQYRATWGGHGSGFYIGDPNLLLAIMGPKVTEYWTQGPAAEKASERLGSTERGQQLMAQHMTIFPTCSFLPGINTIRAWHPRGPNEIEVWAFTVVDADAPEEMKEEYRQQTLRTFSAGGVFEQDDGENWVEIQQVLRGHKARSRPFNAEMGLGQTDSDNPDYPGTISYVYSEEAARGLYTQWVRMMTSPDWAALDATRPAVSESTHT bpha2_rhojr Biphenyl 2,3-dioxygenase subunit beta bphA2 bphAb RHA1_ro08059 Biphenyl dioxygenase system, oxygenase component subunit beta Terminal oxygenase component of biphenyl dioxygenase, small subunit protein protein rhosr Rhodococcus sp. (strain RHA1) MIDAESPTTAFRTKPAPVDPSLQHEIEQFYYWEAKLLNDRRFQEWFDLLAEDIHYFMPIRTTRIMRETAQEYSGAREYAHFDDNAQMMRGRLRKITSDVSWSENPASRTRHVISNVMIVDGEKPGEYHVSSVFIVYRNRLERQLDIFAGERKDILRRTGSEAGFELAKRTILIDQSTILSNNLSFFF bpha1-bpha2-1 Biphenyl dioxygenase (bpha1a2) derived from rhodococcus sp. strain rha1 515050 N/A 515051 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false rhoer Rhodococcus erythropolis Arthrobacter picolinophilus Stoichiometry: 3.0 N/A 515052 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false rhoer Rhodococcus erythropolis Arthrobacter picolinophilus Stoichiometry: 3.0 direct interaction direct interaction false false false hexameric, multimeric working 83.300%, free 79.900% 2.2A bpha1-bpha2-2 Biphenyl dioxygenase (bpha1a2) in complex with the substrate 515050 N/A 515051 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false rhoer Rhodococcus erythropolis Arthrobacter picolinophilus Stoichiometry: 3.0 N/A 515052 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false rhoer Rhodococcus erythropolis Arthrobacter picolinophilus Stoichiometry: 3.0 direct interaction direct interaction false false false hexameric, multimeric working 81.600%, free 76.600% 2.6A