eF-site ID 2wc0-B PDB Code 2wc0 Chain B 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 B:  NNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPT TDKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYP KENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGAL DRFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRLF QLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELL KFHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKN VPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDL QKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGG QKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLR AEGPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILH YYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVS KSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKF KLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFK QDDKFFLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKD SLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILL KKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHA MYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSR LHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQ LVRYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQST SENMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANG IQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAF QKHIQALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDN TEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLARE MNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPHI Description Functional site 1) chain B residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN B 3012 source : AC2 2) chain B residue 112 type sequence H description BINDING SITE FOR RESIDUE ZN B 3012 source : AC2 3) chain B residue 189 type sequence E description BINDING SITE FOR RESIDUE ZN B 3012 source : AC2 4) chain B residue 201 type sequence L description BINDING SITE FOR RESIDUE DIO B 3013 source : AC4 5) chain B residue 205 type sequence E description BINDING SITE FOR RESIDUE DIO B 3013 source : AC4 6) chain B residue 477 type sequence R description BINDING SITE FOR RESIDUE DIO B 3013 source : AC4 7) chain B residue 479 type sequence A description BINDING SITE FOR RESIDUE DIO B 3013 source : AC4 8) chain B residue 329 type sequence N description BINDING SITE FOR RESIDUE DIO B 3014 source : AC7 9) chain B residue 418 type sequence N description BINDING SITE FOR RESIDUE DIO B 3014 source : AC7 10) chain B residue 453 type sequence E description BINDING SITE FOR RESIDUE DIO B 3014 source : AC7 11) chain B residue 301 type sequence L description BINDING SITE FOR RESIDUE DIO B 3015 source : AC8 12) chain B residue 387 type sequence V description BINDING SITE FOR RESIDUE DIO B 3015 source : AC8 13) chain B residue 388 type sequence E description BINDING SITE FOR RESIDUE DIO B 3015 source : AC8 14) chain B residue 513 type sequence W description BINDING SITE FOR RESIDUE DIO B 3015 source : AC8 15) chain B residue 312 type sequence N description BINDING SITE FOR RESIDUE DIO B 3016 source : BC1 16) chain B residue 358 type sequence T description BINDING SITE FOR RESIDUE DIO B 3016 source : BC1 17) chain B residue 377 type sequence V description BINDING SITE FOR RESIDUE DIO B 3016 source : BC1 18) chain B residue 378 type sequence D description BINDING SITE FOR RESIDUE DIO B 3016 source : BC1 19) 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 20) 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 21) 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 22) 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 23) chain B residue 336 type BINDING sequence H description in the exosite source Swiss-Prot : SWS_FT_FI3 24) chain B residue 359 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18986166 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 429 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 895 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P35559 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 192 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7 source Swiss-Prot : SWS_FT_FI6 28) 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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