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-Structure paper
Title | The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. |
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Journal, issue, pages | J. Biol. Chem., Vol. 288, Page 28514-28523, Year 2013 |
Publish date | Sep 5, 2012 (structure data deposition date) |
![]() | Weber, B.W. / Kimani, S.W. / Varsani, A. / Cowan, D.A. / Hunter, R. / Venter, G.A. / Gumbart, J.C. / Sewell, B.T. |
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Methods | X-ray diffraction |
Resolution | 1.1 - 1.9 Å |
Structure data | ![]() PDB-4gyl: ![]() PDB-4gyn: ![]() PDB-4kzf: ![]() PDB-4lf0: |
Chemicals | ![]() ChemComp-ROP: ![]() ChemComp-CL: ![]() ChemComp-HOH: |
Source |
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![]() | HYDROLASE / amidase / catalytic tetrad / amidase mechanism / acrylamide / Michael Adduct / active site / chloride ion / cysteine 166 oxidation / alpha-beta-beta-alpha sandwich |