eF-site ID 2jbu-B PDB Code 2jbu Chain B 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 B:  PAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTD KSSAALDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYPKE NEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDR FAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQL EKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKF HSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVP LPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQK YYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQK EGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAE GPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYY PLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKS FEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKL PTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQD DKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSL NEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKK IIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMY YLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLH IEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLV RYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSE NMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGIQ GLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQK HIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTE VAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMD SCPVSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHINFMA A Description Functional site 1) chain B residue 201 type sequence L description binding site for residue DIO B 1101 source : AC2 2) chain B residue 205 type sequence E description binding site for residue DIO B 1101 source : AC2 3) chain B residue 208 type sequence T description binding site for residue DIO B 1101 source : AC2 4) chain B residue 477 type sequence R description binding site for residue DIO B 1101 source : AC2 5) chain B residue 479 type sequence A description binding site for residue DIO B 1101 source : AC2 6) 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 7) 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 8) 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 9) 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 10) chain B residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 11) chain B residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 13) chain B residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 14) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 15) 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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