eF-site ID 2jbu-A PDB Code 2jbu Chain A click to enlarge Title Crystal structure of human insulin degrading enzyme complexed with co- purified peptides. Classification HYDROLASE Compound INSULIN-DEGRADING ENZYME Source (2JBU) Sequence A:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT DKSSAALDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYPK ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD RFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQ LEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK FHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNV PLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQ KYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQ KEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRA EGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHY YPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSK SFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFK LPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQ DDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDS LNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLK KIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAM YYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRL HIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQL VRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTS ENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGI QGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQ KHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNT EVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREM DSCPVLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINF MAA Description Functional site 1) chain A residue 201 type sequence L description binding site for residue DIO A 1101 source : AC1 2) chain A residue 204 type sequence L description binding site for residue DIO A 1101 source : AC1 3) chain A residue 205 type sequence E description binding site for residue DIO A 1101 source : AC1 4) chain A residue 208 type sequence T description binding site for residue DIO A 1101 source : AC1 5) chain A residue 302 type sequence Y description binding site for residue DIO A 1101 source : AC1 6) chain A residue 477 type sequence R description binding site for residue DIO A 1101 source : AC1 7) chain A residue 479 type sequence A description binding site for residue DIO A 1101 source : AC1 8) chain A residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 9) chain A residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 10) chain A residue 697 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 11) 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 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 A residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 17) chain A residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5

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