eF-site ID 5wob-C PDB Code 5wob Chain C click to enlarge Title Crystal Structure Analysis of Fab1-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Insulin Classification HYDROLASE Compound Insulin-degrading enzyme Source (5WOB) Sequence C:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPK ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD RFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRLFQ LEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK FHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNV PLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQ KYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQ KEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRA EGPQEWVFQELKDLNAVAFRFKDKERPRGYTSIAGILHYY PLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKS FEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKL PTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQD DKFFLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSL NEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKK IIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMY YLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLH IEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLV RYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSE NMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQ GLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQK HIQALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDNTE VAYLKTLTKDIIKFYKEMLAVDAPRRHKVSVHVLAREMDS APALPQPEVIQNMTEFKRGLPLFPLVKPHI Description Functional site 1) chain C residue 108 type sequence H description binding site for residue ZN C 1101 source : AC3 2) chain C residue 112 type sequence H description binding site for residue ZN C 1101 source : AC3 3) chain C residue 189 type sequence E description binding site for residue ZN C 1101 source : AC3 4) chain C residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 5) chain C residue 697 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 6) chain C 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 7) chain C 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 8) chain C 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 9) chain C 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 10) chain C residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 11) chain C residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 12) chain C residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 13) chain C residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5

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