eF-site ID 2wc0-A PDB Code 2wc0 Chain A click to enlarge Title crystal structure of human insulin degrading enzyme in complex with iodinated insulin Classification HYDROLASE/HORMONE Compound INSULIN-DEGRADING ENZYME Source null (INS_HUMAN) Sequence A:  NNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPT TDKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYP KENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGAL DRFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRLF QLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELL KFHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKN VPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDL QKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGG QKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLR AEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILH YYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVS KSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKF KLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFK QDDKFFLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKD SLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILL KKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHHAM YYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRL HIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQL VRYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTS ENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGI QGLRFIIQSEKPPYLESRVEAFLITMEKSIEDMTEEAFQK HIQALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDNTE VAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMN LSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHI Description Functional site 1) chain A residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN A 3012 source : AC1 2) chain A residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN A 3012 source : AC1 3) chain A residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN A 3012 source : AC1 4) chain A residue 461 type sequence P description BINDING SITE FOR RESIDUE DIO A 3013 source : AC3 5) chain A residue 462 type sequence D description BINDING SITE FOR RESIDUE DIO A 3013 source : AC3 6) chain A residue 465 type sequence E description BINDING SITE FOR RESIDUE DIO A 3013 source : AC3 7) chain A residue 639 type sequence P description BINDING SITE FOR RESIDUE DIO A 3013 source : AC3 8) chain A residue 529 type sequence E description BINDING SITE FOR RESIDUE DIO A 3014 source : AC5 9) chain A residue 201 type sequence L description BINDING SITE FOR RESIDUE DIO A 3015 source : AC6 10) chain A residue 204 type sequence L description BINDING SITE FOR RESIDUE DIO A 3015 source : AC6 11) chain A residue 205 type sequence E description BINDING SITE FOR RESIDUE DIO A 3015 source : AC6 12) chain A residue 302 type sequence Y description BINDING SITE FOR RESIDUE DIO A 3015 source : AC6 13) chain A residue 477 type sequence R description BINDING SITE FOR RESIDUE DIO A 3015 source : AC6 14) chain A residue 388 type sequence E description BINDING SITE FOR RESIDUE DIO A 3016 source : AC9 15) 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 16) 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 17) 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 18) 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 19) chain A 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 A residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 22) chain A residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 24) chain A residue 697 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6

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