4GYL
The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine
Summary for 4GYL
Entry DOI | 10.2210/pdb4gyl/pdb |
Related | 4GYN |
Descriptor | Aliphatic amidase, PROPIONAMIDE, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | amidase, catalytic tetrad, amidase mechanism, acrylamide, michael adduct, hydrolase |
Biological source | Bacillus sp. |
Total number of polymer chains | 1 |
Total formula weight | 38733.42 |
Authors | Weber, B.W.,Sewell, B.T.,Kimani, S.W.,Varsani, A.,Cowan, D.A.,Hunter, R. (deposition date: 2012-09-05, release date: 2013-08-21, Last modification date: 2014-02-05) |
Primary citation | Weber, B.W.,Kimani, S.W.,Varsani, A.,Cowan, D.A.,Hunter, R.,Venter, G.A.,Gumbart, J.C.,Sewell, B.T. The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J.Biol.Chem., 288:28514-28523, 2013 Cited by PubMed: 23946488DOI: 10.1074/jbc.M113.503284 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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