eF-site ID 5wob-H PDB Code 5wob Chain H 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 H:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT DKSSAALDVHIGSLSDPPNAGLSHFLQHMLFLGTKKYPNE YSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFA QFFLSPLFDEAKDREVNAVDSEHEKNVMNDAWRLFQLEKA TGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSA YYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPE FPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYK SNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGA RGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQ EWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLE EVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEG KTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTK NEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKF FLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEY AYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIE KMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLR LLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEA LLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYR EVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSENMF LELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLR FIIQSEKPPHYLESRVEAFLITMEKSIEFQKHIQALAIRR LDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTK EDIIKFYKEMLAVDAPRRHKVSVHVLARAPALPQPEVIQN MTEFKRGLPLFPLVKP Description Functional site 1) chain H residue 108 type sequence H description binding site for residue ZN H 1101 source : AC8 2) chain H residue 112 type sequence H description binding site for residue ZN H 1101 source : AC8 3) chain H residue 189 type sequence E description binding site for residue ZN H 1101 source : AC8 4) chain H 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 5) chain H 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 6) chain H 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 7) chain H 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 H residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 9) chain H residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 10) chain H residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 11) chain H residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 12) chain H residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 13) chain H residue 697 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6

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