eF-site ID 3e50-ABCD PDB Code 3e50 Chain A, B, C, D click to enlarge Title Crystal structure of human insulin degrading enzyme in complex with transforming growth factor-alpha Classification Hydrolase/Hormone Compound Insulin-degrading enzyme Source Homo sapiens (Human) (TGFA_HUMAN) Sequence A:  NNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPT TDKSSAALDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYP KENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGAL DRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLF QLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELL KFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKN VPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDL QKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGG QKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLR AEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILH YYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVS KSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKF KLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFK QDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKD SLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILL KKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHA MYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSR LHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQ LVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQST SENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANG IQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAF QKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDN TEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLARE MDSCPVVGNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKP H B:  PAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTD KSSAALDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYPKE NEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDR FAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQL EKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKF HSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVP LPEFPEHPQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKY YKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKE GARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEG PQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYP LEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSF EGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLP TKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDD KFFLPKACLNFEFFSPFAYVDPLHCNMALYLELLKDSLNE YAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKII EKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYL RLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIE ALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRY REVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENM FLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGQGLR FIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQ ALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAY LKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMSCPV VGNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPH C:  VVSHF D:  VVSHFDSHTQ Description Functional site 1) chain A residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 2) chain A residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 3) chain A residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 4) chain B residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN D 51 source : AC2 5) chain B residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN D 51 source : AC2 6) chain B residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN D 51 source : AC2 7) chain D residue 12 type sequence H description BINDING SITE FOR RESIDUE ZN D 51 source : AC2 8) chain D residue 13 type sequence T description BINDING SITE FOR RESIDUE ZN D 51 source : AC2 9) 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 10) 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 11) 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 12) 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 13) 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 14) 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 15) 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 16) 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 17) chain A residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 18) chain B residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 19) chain A residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 21) chain B residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 22) chain B residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 697 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 27) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 28) 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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