IntAct European Bioinformatics Institute IntAct intact 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 https://www.ebi.ac.uk European Bioinformatics Institute (EMBL-EBI), Wellcome Genome Campus, Hinxton, Cambridge, CB10 1SD, United Kingdom. Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method odpb_human Pyruvate dehydrogenase E1 component subunit beta, mitochondrial PDHB PHE1B protein protein human Homo sapiens Human MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI AB459B1259FBDBD3 magnesium(2+) Magnesium(2+) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) odpa_human Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial PDHE1-A type I PDHA1 PHE1A protein protein human Homo sapiens Human MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS 4D685BBE44A92D4B thiamine(1+) diphosphate(3-) thiamine(1+) diphosphate(3-) thiamine diphosphate thiamine diphosphate dianion thiamine diphosphate(2-) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) AYEKOFBPNLCAJY-UHFFFAOYSA-L AYEKOFBPNLCAJY-UHFFFAOYSA-L e1_pdc_human pyruvate dehydrogenase E1 heterotetramer Pyruvate dehydrogenase E1 heterotetramer pyruvate dehydrogenase E1 complex E1 PDHE1 pyruvate dehydrogenase (E1) E1p 2xPDHA1:2xPDHB 5 cofactor cofactor coenzyme PDHA1 binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 enzyme enzyme pdhb binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain thiamine(1+) diphosphate(3-) binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 2 enzyme enzyme pdha1 binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain thiamine(1+) diphosphate(3-) binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain 3 cofactor cofactor coenzyme 5 cofactor cofactor coenzyme PDHB binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 8 11 13 10 17 14 direct interaction direct interaction human Homo sapiens Human stable complex stable complex physical interaction evidence used in manual assertion physical interaction evidence used in manual assertion IPI inferred from physical interaction The pyruvate dehydrogenase complex (PDC) catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Eukaryotic PDC is a highly organized multienzyme complex with the core structure formed by 60 subunits of dihydrolipoamide acetyltransferase (E2) and 12 monomers of dihydrolipoamide dehydrogenase-binding protein (E3BP) to which other components of the complex are bound: 20-30 heterotetramers (alpha2beta2) of pyruvate dehydrogenase (E1), 6-12 homodimers of dihydrolipoamide dehydrogenase (E3), 1-2 homo (or hetero) dimers of pyruvate dehydrogenase kinase and 2-3 heterodimers of phosphopyruvate dehydrogenase phosphatase. E1 catalyzes the first irreversible and rate-limiting step in the PDC catalyzed reactions, i.e. the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvic acid with formation of 2-a-hydroxyethylidene-TPP and carbon dioxide and reductive acetylation of lipoyl moieties of E2. Heterotetrameric E1 has two active sites that interact with each other during catalysis, each using TPP and magnesium ion as cofactors and each formed on the interface between the alpha and beta subunits. Molecular mass = 154 kDa Heterotetramer