eF-site ID 5foa-ABCDEF PDB Code 5foa Chain A, B, C, D, E, F click to enlarge Title Crystal Structure of Human Complement C3b in complex with DAF (CCP2-4) Classification LIPID BINDING 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 AKDQLTCNKFDLKVTIKPAPNTMILEICTRYRGDQDATMS ILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDR NTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYA YYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQ KSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEY IMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKH YLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEE NQKQCQDLGAFTESMVVFGCPN 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 EDAVDAERLKHLIVTPSGCGEENMIGMTPTVIAVHYLDET EQWEKFGLEKRQGALELIKKGYTQQLAFRQPSSAFAAFVK RAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEK QKPDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISL QEAKDICEEQVNSLPGSITKAGDFLEANYMNLQRSYTVAI AGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVE ATSYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQA TFMVFQALAQYQKDAPDHQELNLDVSLQLPSRSSKITHRI HWESASLLRSEETKENEGFTVTAEGKGQGTLSVVTMYHAK AKDQLTCNKFDLKVTIKPAPNTMILEICTRYRGDQDATMS ILDISMMTGFAPDTDDLKQLANGVDRYISKYELDKAFSDR NTLIIYLDKVSHSEDDCLAFKVHQYFNVELIQPGAVKVYA YYNLEESCTRFYHPEKEDGKLNKLCRDELCRCAEENCFIQ KSDDKVTLEERLDKACEPGVDYVYKTRLVKVQLSNDFDEY IMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKH YLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEE NQKQCQDLGAFTESMVVFGCPN E:  SCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRRE PSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDV PGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDP LPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKG FTMIGEHSIYCTVNNDEGEWSGPPPECRG F:  SCEVPTRLNSASLKQPYITQNYFPVGTVVEYECRPGYRRE PSLSPKLTCLQNLKWSTAVEFCKKKSCPNPGEIRNGQIDV PGGILFGATISFSCNTGYKLFGSTSSFCLISGSSVQWSDP LPECREIYCPAPPQIDNGIIQGERDHYGYRQSVTYACNKG FTMIGEHSIYCTVNNDEGEWSGPPPECRG Description Functional site 1) chain B residue 1617 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 2) chain D residue 1617 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 source Swiss-Prot : SWS_FT_FI6 3) chain B residue 1010 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 4) chain B residue 1013 type CROSSLNK sequence E description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 5) chain D residue 1010 type CROSSLNK sequence C description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 6) chain D residue 1013 type CROSSLNK sequence E description Isoglutamyl cysteine thioester (Cys-Gln) source Swiss-Prot : SWS_FT_FI7 7) chain D residue 954 type SITE sequence R description Cleavage; by factor I => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 8) chain B residue 954 type SITE sequence R description Cleavage; by factor I => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 9) chain D residue 1303 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 10) chain D residue 1320 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 11) chain B residue 1303 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 12) chain B residue 1320 type SITE sequence R description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 13) chain C residue 38 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 14) chain C residue 70 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 15) chain C residue 297 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 16) chain C residue 303 type SITE sequence S description Cleavage; by factor I source Swiss-Prot : SWS_FT_FI2 17) 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 18) chain D 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 19) chain D residue 1321 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 20) chain D residue 1573 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 21) chain B residue 968 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 1321 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 1573 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 24) chain D residue 968 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI4 25) 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 26) chain D 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 27) chain B residue 1007-1015 type prosite sequence PSGCGEENM description ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PsGCGEEnM source prosite : PS00477

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