eF-site ID 5fo9-ABCDEF PDB Code 5fo9 Chain A, B, C, D, E, F click to enlarge Title Crystal Structure of Human Complement C3b in Complex with CR1 (CCP15- 17) Classification LIPID BINDING PROTEIN 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 EDAVDAERLKHLIVTPSGCGEENMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI QKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDE YIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKK HYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDE ENQKQCQDLGAFTESMVVFGCPN C:  GHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGR PFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITD IQVGSRINYSCTTGHRLIGHSSAECILSGNTAHWSTKPPI CQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNLGSR GRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCII D:  SPMYSIITPNILRLESEETMVLEAHDAQGDVPVTVTVHDF PGKKLVLSSEKTVLTPATNHMGNVTFTIPANREFKSEKGR NKFVTVQATFGTQVVEKVVLVSLQSGYLFIQTDKTIYTPG STVLYRIFTVNHKLLPVGRTVMVNIENPEGIPVKQDSLSS QNQLGVLPLSWDIPELVNMGQWKIRAYYENSPQQVFSTEF EVKEYVLPSFEVIVEPTEKFYYIYNEKGLEVTITARFLYG KKVEGTAFVIFGIQDGEQRISLPESLKRIPIEDGSGEVVL SRKVLLDGVQNPRAEDLVGKSLYVSATVILHSGSDMVQAE RSGIPIVTSPYQIHFTKTPKYFKPGMPFDLMVFVTNPDGS PAYRVPVAVQGEDTVQSLTQGDGVAKLSINTHPSQKPLSI TVRTKKQELSEAEQATRTMQALPYSTVGNSNNYLHLSVLR TELRPGETLNVNFLLRMDRAHEAKIRYYTYLIMNKGRLLK AGRQVREPGQDLVVLPLSITTDFIPSFRLVAYYTLIGASG QREVVADSVWVDVKDSCVGSLVVKSGQSEDRQPVPGQQMT LKIEGDHGARVVLVAVDKGVFVLNKKNKLTQSKIWDVVEK ADIGCTPGSGKDYAGVFSDAGLTFTSSSGQQTAQRAELQC PQ E:  DEDIIAEENIVSRSEFPESWLWNVEDLKEPPKNGISTKLM NIFLKDSITTWEILAVSMSDKKGICVADPFEVTVMQDFFI DLRLPYSVVRNEQVEIRAVLYNYRQNQELKVRVELLHNPA FCSLATTKRRHQQTVTIPPKSSLSVPYVIVPLKTGLQEVE VKAAVYHHFISDGVRKSLKVVPEGIRMNKTVAVRTLDPER LGREGVQKEDIPPADLSDQVPDTESETRILLQGTPVAQMT EDAVDAERLKHLIVTPSGCGEENMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPKNTMILEICTRYRGDQDATM SILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSD RNTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVY AYYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFI QKSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDE YIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKK HYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDE ENQKQCQDLGAFTESMVVFGCPN F:  GHCQAPDHFLFAKLKTQTNASDFPIGTSLKYECRPEYYGR PFSITCLDNLVWSSPKDVCKRKSCKTPPDPVNGMVHVITD IQVGSRINYSCTTGHRLIGHSSAECILSGNTAHWSTKPPI CQRIPCGLPPTIANGDFISTNRENFHYGSVVTYRCNLGSR GRKVFELVGEPSIYCTSNDDQVGIWSGPAPQCII Description Functional site 1) chain B residue 968 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 2) chain B residue 1321 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 3) chain B residue 1573 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 4) chain E residue 968 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 5) chain E residue 1321 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 6) chain E residue 1573 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 7) chain B residue 1007-1015 type prosite sequence PSGCGEENM description ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEEnM source prosite : PS00477 8) chain B residue 1617 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 9) chain E residue 1617 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 10) chain B residue 1010 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 11) chain B residue 1013 type CROSSLNK sequence E description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 12) chain E residue 1010 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 13) chain E residue 1013 type CROSSLNK sequence E description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 14) chain C residue 959 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 1028 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 16) chain F residue 959 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 17) chain F residue 1028 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 1303 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 19) chain B residue 1320 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 20) chain E residue 1303 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 21) chain E residue 1320 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 22) chain D residue 38 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 23) chain D residue 70 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 24) chain D residue 297 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 25) chain D residue 303 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 26) chain B residue 1663 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 E residue 1663 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 28) chain B residue 939 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 29) chain E residue 939 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

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