Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme in complex with N-cyclohexyl-N'-(iodophenyl)urea, sitting drop vapour diffusion method, 0.005 ml of 12-16 mg/ml protein in 3 mM DTT, 0.1 M sodium phosphate, pH 7.4, is mixed with 0.005 ml precipitation solution containing 0.1 M Tris, pH 9.0, 30% w/v PEG 4000, and 0.2 M Li2SO4, versus 1 ml reservoir of precipitation solution, 4Ā°C, 10 days, soaking of crystals in inhibitor solution and n-hexadecyl-beta-D-maltoside, X-ray diffraction structure determination and analysis at 2.35 A resolution, modeling | Homo sapiens |
sitting drop vapour diffusion method, X-ray crystal structure determined at 2.6 A resolution, structure of the complex with the inhibitor N-cyclohexyl-NĀ-(iodophenyl)urea determine at 2.35 A resolution | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
N-cyclohexyl-N'-(iodophenyl)urea | binding structure at the C-terminus | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P34913 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
an epoxide + H2O = a glycol | the C-terminal part harbors the epoxide hydrolase activity, the phosphatase activity of the enzyme is located at the N-terminal part of EC 3.1.3.76, both catalytic sites act independently, the epoxide hydrolase reaction proceeds though an alkyl-enzyme intermediate involving the catalytic Asp333, and hydrogen bonds with Tyr381 and Tyr465, reaction mechanism, structure-mechanism relationship | Homo sapiens |
Subunits | Comment | Organism |
---|---|---|
More | the 25 kDa C-terminal part, with a hydrolase alpha/beta-fold, harbors the epoxide hydrolase activity, the enzyme's phosphatase activity of EC3.1.3.76 is located at the 35 kDa N-terminal part which has a different alpha/beta-fold, quarternary structure analysis, structure-mechanism relationship | Homo sapiens |
Synonyms | Comment | Organism |
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More | see also EC 3.1.3.76 | Homo sapiens |