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3.4.21.46: complement factor D

This is an abbreviated version!
For detailed information about complement factor D, go to the full flat file.

Word Map on EC 3.4.21.46

Reaction

selective cleavage of Arg-/-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor =

Synonyms

28 kDa protein, adipocyte, Adipsin, alternative complement pathway component Factor D, C3 convertase activator, C3 proactivator convertase, CFD, complement factor D/adipsin and kallikrein-like serine protease, convertase, C3 proactivator, Df, Df protein, endogenous vascular elastase, esterase, properdin factor D, factor D, factor D (complement), fD, PDGF-D, platelet-derived growth factor D, PoDAK, vascular endothelial growth factor, vascular endothelial growth factor D, VEGF-D

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.46 complement factor D

Crystallization

Crystallization on EC 3.4.21.46 - complement factor D

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of profactor D
in complex with inhibitors, sitting drop vapor diffusion method, using 25% (w/v) PEGME 3350, 100 mM Bis-Tris pH 5.5 or 30% (w/v) PEG MME 2000, 0.1 M thiocyanate
in complex with inhibitors, vapor diffusion method, using 22 or 27% (w/v) PEG3350, 50 mM NaCl and 100 mM HEPES/NaOH, pH 7.5 at 20°C
purified enzyme in complex with anti-factor D Fab fragment, sitting drop vapor diffusion method, 30 mg/ml protein in 20 mM HEPES, pH 7.2, and 200 mM NaCl, is mixed with an equal volume of crystallization buffer containing 0.1 M Tris-HCl, pH 8.5, 0.2 M ammonium phosphate, 50% 2-methyl-2,4-pentanediol, and 0.01 M hexamine cobalt(III) chloride, 6 days, 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution
S183A mutant protein in complex with pro-convertase C3bB
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structure of diisopropyl fluorophosphate-inhibited factor D
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structure of native factor D and a complex formed with isatoic anhydride inhibitor
wild type and mutant factor D, expression in CHO cells
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wild-type enzyme, mutants R202A and S81Y/T198S/S199W, and enzyme mutant S183A in ternary complex with C3bB, hanging drop vapour diffusion technique, mixing of 10 mg/ml protein solution with reservoir solution consisting of 15% w/v PEG 6000, 50 mM MES-NaOH pH 6.0, 18°C, 6 days, X-ray diffraction structure determination and analysis at 1.8 A, 2.8 A, 2.0 A, and 3.5 A resolution, respectively, molecular replacement and ensemble refinement
purified enzyme in complex with anti-factor D Fab fragment, sitting drop vapor diffusion method, 20 mg/ml protein in 20 mM HEPES, pH 7.2, and 200 mM NaCl, is mixed with an equal volume of crystallization buffer containing 0.1 M MES, pH 6.5, 25% PEG monomethyl ether 550, 0.01 M zinc sulfate, and 3% 6-aminohexanoic acid, 1 day, 19°C, X-ray diffraction structure determination and analysis at 2.3 A resolution
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