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3.4.22.59: caspase-6

This is an abbreviated version!
For detailed information about caspase-6, go to the full flat file.

Word Map on EC 3.4.22.59

Reaction

strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-/- =

Synonyms

apoptotic protease Mch-2, C14.005, Cas6, Casp-6, Casp.6, Casp6, caspase 6, caspase-6, caspase-6A, caspase-6B, Csp-6, Csp6, HLcaspase-6, MCH2, Pfcasp-6, VEIDase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.59 caspase-6

Crystallization

Crystallization on EC 3.4.22.59 - caspase-6

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M sodium acetate, pH 4.6, 2 M NaCl, and 3% (v/v) ethanol
in complex with benzyloxycarbonyl-VEID, using 12% (w/v) PEG 3350, 0.2 M sodium malonate pH 4.0
recombinant caspase-6 comprising residues 24–179 and 194–293 after self-cleavage of the zymogen, overall structure of the four caspase-6 p202/p102 tetramers in the asymmetric unit, and caspase-6 in complex with inhibitor Ac-VEID-CHO, hanging-drop vapor diffusion method, mixing of 0.001 ml protein solution containing 20 mM sodium acetate, pH 5.5, 50 mM NaCl, and 0.5 mM Tris(hydroxypropyl)phosphine with 0.001 ml of reservoir solution consisting of 3.3 M sodium nitrate, 0.1 M Tris, pH 7.4, 0.5% ethyl acetate, and 5 mM Tris(hydroxypropyl)phosphine, and microseeding, 1 week, 20°C, X-ray diffraction structure determination and analysis at 2.53 A resolution, molecular replacement, structure comparisons, overview
sitting drop vapour diffusion method