eF-site ID 2wby-ABCDEF PDB Code 2wby Chain A, B, C, D, E, F click to enlarge Title Crystal structure of human insulin-degrading enzyme in complex with insulin Classification HYDROLASE/HORMONE Compound INSULIN-DEGRADING ENZYME Source Homo sapiens (Human) (INS_HUMAN) Sequence A:  MNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDP TTDKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKY PKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGA LDRFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRL FQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQEL LKFHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENK NVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPD LQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVG GQKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKL RAEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGIL HYYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIV SKSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGK FKLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWF KQDDKFFLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLK DSLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPIL LKKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQH AMYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLS RLHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPS QLVRYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQS TSENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRAN GIQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEA FQKHIQALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRD NTEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAR EMDSNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHI B:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPK ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD RFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRLFQ LEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK FHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNV PLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQ KYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQ KEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRA EGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHY YPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSK SFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFK LPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQ DDKFFLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDS LNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLK KIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAM YYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRL HIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQL VRYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTS ENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGI QGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQ KHIQALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDNT EVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREM DNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHI C:  GIVEQCCTSICSLYQLENYC D:  FVNQHLCGSHLVEALYLV E:  GIVEQCCTSICSLYQLENYC F:  FVNQHLCGSHLVEALYLVC Description Functional site 1) chain B residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN B 3012 source : AC1 2) chain B residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN B 3012 source : AC1 3) chain B residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN B 3012 source : AC1 4) chain F residue 1 type sequence F description BINDING SITE FOR RESIDUE ZN B 3012 source : AC1 5) chain A residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN A 3012 source : AC2 6) chain A residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN A 3012 source : AC2 7) chain A residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN A 3012 source : AC2 8) chain D residue 1 type sequence F description BINDING SITE FOR RESIDUE ZN A 3012 source : AC2 9) chain C residue 6-20 type prosite sequence CCTSICSLYQLENYC description INSULIN Insulin family signature. CCTSiCSlyqLenyC source prosite : PS00262 10) chain A residue 111 type ACT_SITE sequence Q 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 11) chain B residue 111 type ACT_SITE sequence Q 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 12) chain A residue 108 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 13) chain A residue 112 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 14) chain A residue 189 type BINDING sequence E 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 15) chain B residue 108 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 16) chain B residue 112 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 17) chain B residue 189 type BINDING sequence E 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 18) chain A residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 19) chain B residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 20) chain A residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 24) chain B residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 25) chain B residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 697 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 28) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 29) chain B residue 697 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6

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