3.4.21.41: complement subcomponent C1r
This is an abbreviated version!
For detailed information about complement subcomponent C1r, go to the full flat file.
Word Map on EC 3.4.21.41
Reaction
Selective cleavage of Lys(or Arg)-/-Ile bond in complement subcomponent C1s to form C_overbar_1s_ (EC 3.4.21.42) =
Synonyms
activated complement C1r, C1r, C1r protease, C1r serine protease, C1r-LP, C1rbar-esterase, complement C1r subcomponent-like protein, complement C1r, activated, complement protease C1r, complement subcomponent 1r, CUB, multiprotein complex C1, proteases C1r, serine protease C1r, Xld, xolloid
ECTree
3.4.21.41 complement subcomponent C1rAdvanced search results
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results (Crystallization
Crystallization on EC 3.4.21.41 - complement subcomponent C1r
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
complex between the CUB1-EGF-CUB2 domains of C1r and C1s, sitting drop vapor diffusion method, in imidazole buffer at pH 8.0 with PEG 8000 as the precipitant
hanging drop vapour diffusion method, crystal structure of two fragments from the human C1r catalytic domain, each encompassing the second complement control protein CCP2 module and the SP domain. The wild-type species has an active structure, whereas the S637A mutant is a zymogen
hanging drop vapour diffusion, crystal structure of a mutated proenzyme form of the catalytic domain of human C1r, and the serine protease domain solved and refined to 2.9 A resolution
purified recombinant isolated active catalytic region forming a dimer in a head-to-tail fashion, complex of enzyme and product, hanging drop vapour diffusion method, 15°C, mixing of 0.008 ml protein solution, containing 0.2 mg/ml protein, 20 mM Tris-HCl, pH 7.4, and 130 mM NaC, with 0.008 ml reservoir solution containing 14% w/v PEG 6000, 0.2 M NaCl, 10% v/v glycerol, and 0.1 M Tris-HCl, pH 7.4, cryoprotection of crystals in 20% glycerol, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement
