eF-site ID 2rio-AB PDB Code 2rio Chain A, B click to enlarge Title Structure of the dual enzyme Ire1 reveals the basis for catalysis and regulation of non-conventional splicing Classification HYDROLASE, TRANSFERASE Compound Serine/threonine-protein kinase/endoribonuclease IRE1 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (IRE1_YEAST) Sequence A:  NFEQSLKNLVVSEKILGYGSSGTVVFQGSFQGRPVAVKRM LIDFCDIALMEIKLLTESDDHPNVIRYYCSETTDRFLYIA LELCNLNLQDLVESKYNPISLLRQIASGVAHLHSLKIIHR DLKPQNILVSTSSRFTADQQTGAENLRILISDFGLCKKLD STSGWRAPELLEESNNLQTKRRLTRSIDIFSMGCVFYYIL SKGKHPFGDKYSRESNIIRGIFSLDEMKCLHDRSLIAEAT DLISQMIDHDPLKRPTAMKVLRHPLFWPKSKKLEFLLKVS DRLEIENRDPPSALLMKFDAGSDFVIPSGDWTVKFDKTFM DRKYHSSKLMDLLRALRNKYHHFMDLPEDIAELMGPVPDG FYDYFTKRFPNLLIGVYMIVKENLSDDQILREFLYS B:  NFEQSLKNLVVSEKILGYGSSGTVVFQGSFQGRPVAVKRM LIDFCDIALMEIKLLTESDDHPNVIRYYCSETTDRFLYIA LELCNLNLQDLVESYNPISLLRQIASGVAHLHSLKIIHRD LKPQNILVSTSSRFTADQQTGAENLRILISDFGLCKKLDS TSGWRAPELLEESNNLQTKRRLTRSIDIFSMGCVFYYILS KGKHPFGDKYSRESNIIRGIFSLDEMKCLHDRSLIAEATD LISQMIDHDPLKRPTAMKVLRHPLFWPKSKKLEFLLKVSD RLEIENRDPPSALLMKFDAGSDFVIPSGDWTVKFDKTFMD RKYHSSKLMDLLRALRNKYHHFMDLPEDIAELMGPVPDGF YDYFTKRFPNLLIGVYMIVKENLSDDQILREFLYS Description Functional site 1) chain A residue 145 type sequence N description BINDING SITE FOR RESIDUE MG A 1102 source : AC1 2) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE MG A 1102 source : AC1 3) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE SR A 1103 source : AC2 4) chain B residue 145 type sequence N description BINDING SITE FOR RESIDUE MG B 2102 source : AC3 5) chain B residue 171 type sequence D description BINDING SITE FOR RESIDUE MG B 2102 source : AC3 6) chain B residue 171 type sequence D description BINDING SITE FOR RESIDUE SR B 2103 source : AC4 7) chain A residue 24 type sequence G description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 8) chain A residue 25 type sequence Y description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 9) chain A residue 26 type sequence G description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 10) chain A residue 27 type sequence S description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 11) chain A residue 30 type sequence T description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 12) chain A residue 32 type sequence V description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 13) chain A residue 43 type sequence A description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 14) chain A residue 45 type sequence K description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 15) chain A residue 88 type sequence L description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 16) chain A residue 89 type sequence E description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 17) chain A residue 91 type sequence C description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 18) chain A residue 94 type sequence N description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 19) chain A residue 144 type sequence Q description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 20) chain A residue 145 type sequence N description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 21) chain A residue 147 type sequence L description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 22) chain A residue 171 type sequence D description BINDING SITE FOR RESIDUE ADP A 1101 source : AC5 23) chain B residue 24 type sequence G description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 24) chain B residue 25 type sequence Y description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 25) chain B residue 26 type sequence G description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 26) chain B residue 27 type sequence S description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 27) chain B residue 30 type sequence T description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 28) chain B residue 32 type sequence V description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 29) chain B residue 43 type sequence A description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 30) chain B residue 45 type sequence K description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 31) chain B residue 72 type sequence I description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 32) chain B residue 89 type sequence E description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 33) chain B residue 91 type sequence C description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 34) chain B residue 94 type sequence N description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 35) chain B residue 144 type sequence Q description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 36) chain B residue 145 type sequence N description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 37) chain B residue 147 type sequence L description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 38) chain B residue 171 type sequence D description BINDING SITE FOR RESIDUE ADP B 2101 source : AC6 39) chain A residue 136-148 type prosite sequence IIHRDLKPQNILV description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILV source prosite : PS00108 40) chain A residue 140 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 140 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 23 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 23 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 45 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3 45) chain B residue 45 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI3

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