eF-site ID 2win-ABCDEFGHIJKLMNPQ PDB Code 2win Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, P, Q Title C3 convertase (C3bBb) stabilized by SCIN Classification IMMUNE SYSTEM Compound COMPLEMENT C3 BETA CHAIN Source ORGANISM_COMMON: HUMAN; ORGANISM_SCIENTIFIC: HOMO SAPIENS; Sequence A:  SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANRKGRNKFVT VQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLY RIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLG VLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEY VLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEG TAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVL LDGVQRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIV TSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPV AVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQ ELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGE TLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVRE PGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVAD SVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDH GARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTP GSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAA B:  LDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKL MNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFF IDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNP AFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEV EVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPE RLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQM TEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDE TEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSAFVKRAP STWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKP DGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEA KDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGY ALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATS YALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFM VFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWE SASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKD QLTCNKFDLKVTIKPAPETAKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI SDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYI MAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHY LMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEEN QKQCQDLGAFTESMVVFGCPN C:  SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANRKGRNKFVT VQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLY RIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLG VLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEY VLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEG TAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVL LDGVQRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIV TSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPV AVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQ ELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGE TLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVRE PGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVAD SVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDH GARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTP GSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAA D:  LDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKL MNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFF IDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNP AFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEV EVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPE RLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQM TEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDE TEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSAFVKRAP STWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKP DGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEA KDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGY ALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATS YALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFM VFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWE SASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKD QLTCNKFDLKVTIKPAPQDAKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI SDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYI MAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHY LMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEEN QKQCQDLGAFTESMVVFGCPN E:  SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANRKGRNKFVT VQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLY RIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLG VLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEY VLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEG TAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVL LDGVQRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIV TSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPV AVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQ ELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGE TLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVRE PGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVAD SVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDH GARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTP GSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAA F:  LDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKL MNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFF IDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNP AFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEV EVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPE RLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQM TEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDE TEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSAFVKRAP STWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKP DGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEA KDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGY ALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATS YALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFM VFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWE SASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKD QLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATMSIL DISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNT LIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYY NLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKS DDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIM AIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYL MWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQ KQCQDLGAFTESMVVFGCPN G:  SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANRKGRNKFVT VQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLY RIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSSQNQLG VLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEFEVKEY VLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYGKKVEG TAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVLSRKVL LDGVQRAEDLVGKSLYVSATVILHSGSDMVQAERSGIPIV TSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGSPAYRVPV AVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSITVRTKKQ ELSEAEQATRTMQALPYSTVGNSNNYLHLSVLRTELRPGE TLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLKAGRQVRE PGQDLVVLPLSITTDFIPSFRLVAYYTLIGASGQREVVAD SVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMTLKIEGDH GARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTP GSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQCPQPAA H:  LDEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKL MNIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFF IDLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNP AFCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEV EVKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPE RLGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQM TEDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDE TEQWEKFGLEKRQGALELIKKGYTQQLAFRQPSAFVKRAP STWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQKP DGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEA KDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAIAGY ALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEATS YALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFM VFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRIHWE SASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAKAKD QLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATMSIL DISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDRNT LIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYAYY NLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQKS DDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEYIM AIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYL MWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQ KQCQDLGAFTESMVVFGCPN I:  KIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEK VASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQL NEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNR TRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPR EDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDME NLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKI SVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKV SVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVAL IKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQK EELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERD AQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDS GGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHAR DFHINLFQVLPWLKEKLQDEDLGFLAA J:  KIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEK VASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQL NEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNR TRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPR EDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDME NLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKI SVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKV SVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVAL IKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQK EELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERD AQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDS GGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHAR DFHINLFQVLPWLKEKLQDEDLGFLAA K:  KIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEK VASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQL NEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNR TRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPR EDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDME NLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKI SVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKV SVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVAL IKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQK EELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERD AQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDS GGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHAR DFHINLFQVLPWLKEKLQDEDLGFLAA L:  KIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEK VASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQL NEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNR TRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPR EDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDME NLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKI SVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKV SVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVAL IKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQK EELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERD AQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDS GGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHAR DFHINLFQVLPWLKEKLQDEDLGFLAA M:  TSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYK RTIKISGQKAMYALKSKDFKKMSEAKYQLQKIYNEIDEAL KSKY N:  TSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYK RTIKISGQKAMYALKSKDFKKMSEAKYQLQKIYNEIDEAL KSKY P:  TSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYK RTIKISGQKAMYALKSKDFKKMSEAKYQLQKIYNEIDEAL KSKY Q:  TSLPTSNEYQNEKLANELKSLLDELNVNELATGSLNTYYK RTIKISGQKAMYALKSKDFKKMSEAKYQLQKIYNEIDEAL KSKY Description Functional site 1) chain B residue 1595 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 2) chain D residue 1595 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 3) chain F residue 1595 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 4) chain H residue 1595 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 5) chain B residue 988 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 6) chain B residue 991 type CROSSLNK sequence Q description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 7) chain D residue 988 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 8) chain D residue 991 type CROSSLNK sequence Q description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 9) chain F residue 988 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 10) chain F residue 991 type CROSSLNK sequence Q description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 11) chain H residue 988 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 12) chain H residue 991 type CROSSLNK sequence Q description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 13) chain I residue 501 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI1 14) chain I residue 551 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 15) chain I residue 674 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI1 16) chain J residue 501 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI1 17) chain J residue 551 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 18) chain J residue 674 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI1 19) chain K residue 501 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI1 20) chain K residue 551 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 21) chain K residue 674 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI1 22) chain L residue 501 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI1 23) chain L residue 551 type ACT_SITE sequence D description Charge relay system source Swiss-Prot : SWS_FT_FI1 24) chain L residue 674 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI1 25) chain F residue 1281 type CARBOHYD sequence R description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 26) chain F residue 1298 type CARBOHYD sequence R description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 27) chain H residue 1281 type CARBOHYD sequence R description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 28) chain H residue 1298 type CARBOHYD sequence R description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 29) chain I residue 260 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 30) chain J residue 260 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 31) chain K residue 260 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 32) chain L residue 260 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 33) chain E residue 16 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 34) chain E residue 48 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 35) chain E residue 275 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 36) chain E residue 281 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 37) chain G residue 16 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 38) chain G residue 48 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 39) chain G residue 275 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 40) chain G residue 281 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI2 41) chain I residue 266 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:2006911 source Swiss-Prot : SWS_FT_FI3 42) chain J residue 266 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:2006911 source Swiss-Prot : SWS_FT_FI3 43) chain K residue 266 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:2006911 source Swiss-Prot : SWS_FT_FI3 44) chain L residue 266 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:2006911 source Swiss-Prot : SWS_FT_FI3 45) chain F residue 1551 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 46) chain H residue 946 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 47) chain H residue 1299 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 48) chain H residue 1551 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 49) chain I residue 353 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 50) chain J residue 353 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 51) chain K residue 353 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 52) chain L residue 353 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 53) chain D residue 1299 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 54) chain D residue 1551 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 55) chain F residue 946 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 56) chain F residue 1299 type CARBOHYD sequence S description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17310251, ECO:0000269|PubMed:19574954, ECO:0000269|PubMed:6546754 source Swiss-Prot : SWS_FT_FI4 57) chain B residue 917 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150 source Swiss-Prot : SWS_FT_FI5 58) chain D residue 917 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150 source Swiss-Prot : SWS_FT_FI5 59) chain F residue 917 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150 source Swiss-Prot : SWS_FT_FI5 60) chain H residue 917 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17051150 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 985-993 type prosite sequence PSGCGEQNM description ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEQnM source prosite : PS00477 62) chain I residue 497-502 type prosite sequence LTAAHC description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC source prosite : PS00134 63) chain I residue 668-679 type prosite sequence NTCRGDSGGPLI description TRYPSIN_SER Serine proteases, trypsin family, serine active site. NTcrGDSGGPLI source prosite : PS00135

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