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- SASDBZ7: Complement factor 1s in complex with Complement factor 1r -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDBZ7
SampleComplement factor 1s in complex with Complement factor 1r
  • Complement C1r subcomponent (protein), C1r, Homo sapiens
  • Complement C1s subcomponent (protein), C1s, Homo sapiens
Function / homology
Function and homology information


complement subcomponent C_overbar_1r_ / complement subcomponent C_overbar_1s_ / molecular sequestering activity / zymogen activation / Classical antibody-mediated complement activation / Initial triggering of complement / serine-type peptidase activity / complement activation, classical pathway / Regulation of Complement cascade / blood microparticle ...complement subcomponent C_overbar_1r_ / complement subcomponent C_overbar_1s_ / molecular sequestering activity / zymogen activation / Classical antibody-mediated complement activation / Initial triggering of complement / serine-type peptidase activity / complement activation, classical pathway / Regulation of Complement cascade / blood microparticle / immune response / serine-type endopeptidase activity / innate immune response / calcium ion binding / proteolysis / extracellular space / extracellular exosome / extracellular region / identical protein binding
Similarity search - Function
Peptidase S1A, complement C1r/C1S/mannan-binding / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. / Spermadhesin, CUB domain superfamily / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. ...Peptidase S1A, complement C1r/C1S/mannan-binding / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. / Spermadhesin, CUB domain superfamily / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Coagulation Factor Xa inhibitory site / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Epidermal growth factor-like domain. / EGF-like domain signature 2. / EGF-like domain / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
Complement C1r subcomponent / Complement C1s subcomponent
Similarity search - Component
Biological speciesHomo sapiens (human)
Contact author
  • Rasmus Jensen (Aarhus University, Aarhus, Denmark)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #922
Type: atomic / Software: CORALXL / Radius of dummy atoms: 1.90 A / Symmetry: P2 / Chi-square value: 1.68 / P-value: 0.000030
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Complement factor 1s in complex with Complement factor 1r
Specimen concentration: 1.00-6.80 / Entity id: 544 / 545
BufferName: 50 mM TrisHCl, 145 mM NaCl, 3 mM CaCl2 / pH: 7.4
Entity #544Name: C1r / Type: protein / Description: Complement C1r subcomponent / Formula weight: 78.212 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: P00736
Sequence: SIPIPQKLFG EVTSPLFPKP YPNNFETTTV ITVPTGYRVK LVFQQFDLEP SEGCFYDYVK ISADKKSLGR FCGQLGSPLG NPPGKKEFMS QGNKMLLTFH TDFSNEENGT IMFYKGFLAY YQAVDLDECA SRSKSGEEDP QPQCQHLCHN YVGGYFCSCR PGYELQEDTH ...Sequence:
SIPIPQKLFG EVTSPLFPKP YPNNFETTTV ITVPTGYRVK LVFQQFDLEP SEGCFYDYVK ISADKKSLGR FCGQLGSPLG NPPGKKEFMS QGNKMLLTFH TDFSNEENGT IMFYKGFLAY YQAVDLDECA SRSKSGEEDP QPQCQHLCHN YVGGYFCSCR PGYELQEDTH SCQAECSSEL YTEASGYISS LEYPRSYPPD LRCNYSIRVE RGLTLHLKFL EPFDIDDHQQ VHCPYDQLQI YANGKNIGEF CGKQRPPDLD TSSNAVDLLF FTDESGDSRG WKLRYTTEII KCPQPKTLDE FTIIQNLQPQ YQFRDYFIAT CKQGYQLIEG NQVLHSFTAV CQDDGTWHRA MPRCKIKDCG QPRNLPNGDF RYTTTMGVNT YKARIQYYCH EPYYKMQTRA GSRESEQGVY TCTAQGIWKN EQKGEKIPRC LPVCGKPVNP VEQRQRIIGG QKAKMGNFPW QVFTNIHGRG GGALLGDRWI LTAAHTLYPK EHEAQSNASL DVFLGHTNVE ELMKLGNHPI RRVSVHPDYR QDESYNFEGD IALLELENSV TLGPNLLPIC LPDNDTFYDL GLMGYVSGFG VMEEKIAHDL RFVRLPVANP QACENWLRGK NRMDVFSQNM FCAGHPSLKQ DACQGDSGGV FAVRDPNTDR WVATGIVSWG IGCSRGYGFY TKVLNYVDWI KKEMEEED
Entity #545Name: C1s / Type: protein / Description: Complement C1s subcomponent / Formula weight: 74.886 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: P09871
Sequence: EPTMYGEILS PNYPQAYPSE VEKSWDIEVP EGYGIHLYFT HLDIELSENC AYDSVQIISG DTEEGRLCGQ RSSNNPHSPI VEEFQVPYNK LQVIFKSDFS NEERFTGFAA YYVATDINEC TDFVDVPCSH FCNNFIGGYF CSCPPEYFLH DDMKNCGVNC SGDVFTALIG ...Sequence:
EPTMYGEILS PNYPQAYPSE VEKSWDIEVP EGYGIHLYFT HLDIELSENC AYDSVQIISG DTEEGRLCGQ RSSNNPHSPI VEEFQVPYNK LQVIFKSDFS NEERFTGFAA YYVATDINEC TDFVDVPCSH FCNNFIGGYF CSCPPEYFLH DDMKNCGVNC SGDVFTALIG EIASPNYPKP YPENSRCEYQ IRLEKGFQVV VTLRREDFDV EAADSAGNCL DSLVFVAGDR QFGPYCGHGF PGPLNIETKS NALDIIFQTD LTGQKKGWKL RYHGDPMPCP KEDTPNSVWE PAKAKYVFRD VVQITCLDGF EVVEGRVGAT SFYSTCQSNG KWSNSKLKCQ PVDCGIPESI ENGKVEDPES TLFGSVIRYT CEEPYYYMEN GGGGEYHCAG NGSWVNEVLG PELPKCVPVC GVPREPFEEK QRIIGGSDAD IKNFPWQVFF DNPWAGGALI NEYWVLTAAH VVEGNREPTM YVGSTSVQTS RLAKSKMLTP EHVFIHPGWK LLEVPEGRTN FDNDIALVRL KDPVKMGPTV SPICLPGTSS DYNLMDGDLG LISGWGRTEK RDRAVRLKAA RLPVAPLRKC KEVKVEKPTA DAEAYVFTPN MICAGGEKGM DSCKGDSGGA FAVQDPNDKT KFYAAGLVSW GPQCGTYGLY TRVKNYVDWI MKTMQENSTP RED

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.0992 Å
DetectorName: Pilatus 1M
Scan
Title: Complement factor 1s in complex with Complement fa / Measurement date: Dec 8, 2014 / Storage temperature: 4 °C / Cell temperature: 4 °C / Exposure time: 2 sec. / Number of frames: 10 / Unit: 1/nm /
MinMax
Q0.0506 2.5007
ResultType of curve: merged /
ExperimentalStandard
MW297 kDa297 kDa

GuinierGuinier error
Forward scattering, I0389.21 1.02
Radius of gyration, Rg11.64 nm0.36

MinMax
Guinier point1 11

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