eF-site ID 3g6j-ABCDEFGH PDB Code 3g6j Chain A, B, C, D, E, F, G, H click to enlarge Title C3b in complex with a C3b specific Fab Classification IMMUNE SYSTEM Compound Complement C3 beta chain Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGR NKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPG STVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSS QNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEF EVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYG KKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVL SRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAE RSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGS PAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSI TVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLR TELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLK AGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASG QREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMT LKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEK ADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQC PQ B:  DEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLM NIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFI DLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPA FCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVE VKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPER LGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMT EDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPETKNTMILEICTRYRGDQDA TMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAF SDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVK VYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENC FIQKDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDE YIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKK HYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDE ENQKQCQDLGAFTESMVVFGCPN C:  SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGR NKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPG STVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSS QNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEF EVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYG KKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVL SRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAE RSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGS PAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSI TVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLR TELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLK AGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASG QREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMT LKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEK ADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQC PQ D:  DEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLM NIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFI DLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPA FCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVE VKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPER LGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMT EDAVDAERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPETKNTMILEICTRYRGDQDA TMSILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAF SDRNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVK VYAYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENC FIQKDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDE YIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKK HYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDE ENQKQCQDLGAFTESMVVFGCPN E:  DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKP GKAPKLLIYSASFLYSGVPSRFSGSGSGTDFTLTISSLQP EDFATYYCQQSYATLPTFEQGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQG LSSPVTKSFNRGEC F:  EVQLVESGGGLVQPGGSLRLSCAASGFSFTSSSVSWVRQA PGKGLEWVGLIYPYNGFNYYADSVKGRFTISANTSKNTAY LQMNSLRAEDTAVYYCARNALYGSGGYYAMDYWGQGTLVT VSSASTKGPSVFPLAPSSGTAALGCLVKDYFPEPVTVSWN SGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYI CNVNHKPSNTKVDKKVEPKSC G:  DIQMTQSPSSLSASVGDRVTITCRASQDVSTAVAWYQQKP GKAPKLLIYSASFLYSGVPSRFSGSGSGTDFTLTISSLQP EDFATYYCQQSYATLPTFEQGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQG LSSPVTKSFNRGEC H:  EVQLVESGGGLVQPGGSLRLSCAASGFSFTSSSVSWVRQA PGKGLEWVGLIYPYNGFNYYADSVKGRFTISANTSKNTAY LQMNSLRAEDTAVYYCARNALYGSGGYYAMDYWGQGTLVT VSSASTKGPSVFPLAPSSGTAALGCLVKDYFPEPVTVSWN SGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYI CNVNHKPSNTKVDKKVEPKSC Description Functional site 1) chain A residue 505 type sequence P description BINDING SITE FOR RESIDUE CA A 645 source : AC1 2) chain A residue 532 type sequence D description BINDING SITE FOR RESIDUE CA A 645 source : AC1 3) chain A residue 533 type sequence V description BINDING SITE FOR RESIDUE CA A 645 source : AC1 4) chain A residue 535 type sequence D description BINDING SITE FOR RESIDUE CA A 645 source : AC1 5) chain C residue 505 type sequence P description BINDING SITE FOR RESIDUE CA C 645 source : AC2 6) chain C residue 532 type sequence D description BINDING SITE FOR RESIDUE CA C 645 source : AC2 7) chain C residue 533 type sequence V description BINDING SITE FOR RESIDUE CA C 645 source : AC2 8) chain C residue 535 type sequence D description BINDING SITE FOR RESIDUE CA C 645 source : AC2 9) chain B residue 1595 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 10) chain D residue 1595 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 11) chain B residue 988 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 12) chain B residue 991 type CROSSLNK sequence Q description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 13) chain D residue 988 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 14) chain D residue 991 type CROSSLNK sequence Q description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 15) chain D residue 932 type SITE sequence R description Cleavage; by factor I => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 932 type SITE sequence R description Cleavage; by factor I => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 17) chain D residue 1281 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 18) chain D residue 1298 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 19) chain B residue 1281 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 20) chain B residue 1298 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 21) chain C residue 16 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 22) chain C residue 48 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 23) chain C residue 275 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 24) chain C residue 281 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 25) chain B residue 1641 type SITE sequence N description Coordinates Mg2+ for interaction with Complement factor B Bb fragment => ECO:0000269|PubMed:28264884, ECO:0000269|PubMed:31507604 source Swiss-Prot : SWS_FT_FI3 26) chain D residue 1641 type SITE sequence N description Coordinates Mg2+ for interaction with Complement factor B Bb fragment => ECO:0000269|PubMed:28264884, ECO:0000269|PubMed:31507604 source Swiss-Prot : SWS_FT_FI3 27) chain D residue 1299 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 28) chain D residue 1551 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 946 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 30) chain B residue 1299 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 31) chain B residue 1551 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 32) chain D residue 946 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 33) 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 34) 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 35) chain B residue 985-993 type prosite sequence PSGCGEQNM description ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEQnM source prosite : PS00477 36) chain E residue 192-198 type prosite sequence YACEVTH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH source prosite : PS00290 37) chain F residue 194-200 type prosite sequence YICNVNH description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH source prosite : PS00290

Display surface Download Links