eF-site ID 2jg4-AB PDB Code 2jg4 Chain A, B click to enlarge Title Substrate-free IDE structure in its closed conformation Classification HYDROLASE Compound INSULIN DEGRADING ENZYME Source (IDE_HUMAN) Sequence A:  NNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPT TDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYP KENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGAL DRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLF QLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELL KFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKN VPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDL QKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGG QKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLR AEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILH YYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVS KSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKF KLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFK QDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKD SLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILL KKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHA MYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSR LHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQ LVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQST SENMFLELFCQIISEPCFNTLRTKEQLGFIVFSGPRRANG IQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAF QKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDN TEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLARE MDSCPVVGNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKP H B:  PAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTD KSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKE NEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDR FAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQL EKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKF HSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVP LPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQK YYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQK EGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAE GPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYY PLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKS FEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKL PTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQD DKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSL NEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKK IIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMY YLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLH IEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLV RYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSE NMFLELFCQIISEPCFNTLRTKEQLGFIVFSGPRRANGIQ GLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQK HIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTE VAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMS CPVVGNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPH Description Functional site 1) chain A residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN A2012 source : AC1 2) chain A residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN A2012 source : AC1 3) chain A residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN A2012 source : AC1 4) chain B residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN B2012 source : AC2 5) chain B residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN B2012 source : AC2 6) chain B residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN B2012 source : AC2 7) chain B residue 201 type sequence L description BINDING SITE FOR RESIDUE DIO B2013 source : AC3 8) chain B residue 205 type sequence E description BINDING SITE FOR RESIDUE DIO B2013 source : AC3 9) chain B residue 208 type sequence T description BINDING SITE FOR RESIDUE DIO B2013 source : AC3 10) chain B residue 477 type sequence R description BINDING SITE FOR RESIDUE DIO B2013 source : AC3 11) chain A residue 800 type sequence Q description BINDING SITE FOR RESIDUE DIO A2013 source : AC4 12) chain A residue 913 type sequence S description BINDING SITE FOR RESIDUE DIO A2013 source : AC4 13) chain A residue 800 type sequence Q description BINDING SITE FOR RESIDUE DIO A2014 source : AC5 14) chain A residue 839 type sequence R description BINDING SITE FOR RESIDUE DIO A2014 source : AC5 15) chain A residue 840 type sequence A description BINDING SITE FOR RESIDUE DIO A2014 source : AC5 16) chain A residue 841 type sequence N description BINDING SITE FOR RESIDUE DIO A2014 source : AC5 17) chain A residue 842 type sequence G description BINDING SITE FOR RESIDUE DIO A2014 source : AC5 18) chain B residue 800 type sequence Q description BINDING SITE FOR RESIDUE DIO B2014 source : AC6 19) chain B residue 839 type sequence R description BINDING SITE FOR RESIDUE DIO B2014 source : AC6 20) chain B residue 841 type sequence N description BINDING SITE FOR RESIDUE DIO B2014 source : AC6 21) chain B residue 842 type sequence G description BINDING SITE FOR RESIDUE DIO B2014 source : AC6 22) chain A residue 193 type MOD_RES sequence N description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 23) chain A residue 698 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 24) chain B residue 193 type MOD_RES sequence N description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 25) chain B residue 698 type MOD_RES sequence D description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 112 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 112 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 109 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 113 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 190 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 109 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 113 type BINDING sequence M description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 190 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 337 type BINDING sequence L description in the exosite source Swiss-Prot : SWS_FT_FI3 35) chain B residue 337 type BINDING sequence L description in the exosite source Swiss-Prot : SWS_FT_FI3 36) chain A residue 360 type BINDING sequence V description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 37) chain B residue 360 type BINDING sequence V description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 38) chain A residue 430 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 896 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 40) chain B residue 430 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 41) chain B residue 896 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 42) chain A residue 95-118 type prosite sequence GSLSDPPNIAGLSHFCEHMLFLGT description INSULINASE Insulinase family, zinc-binding region signature. GslsdppniaGlSHFCEHMlFlGT source prosite : PS00143

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