4IZU

The E41Q mutant of the amidase from Nesterenkonia sp. AN1 showing the result of Michael addition of acrylamide at the active site cysteine

Summary for 4IZU

• Entry DOI: 10.2210/pdb4izu/pdb
• Related: 3HKX 4IZS 4IZT 4IZV 4IZW
• Descriptor: Amidase, PROPIONAMIDE, prop-2-enamide, ... (4 entities in total)
• Functional Keywords: hydrolase, propionamide, acrylamide (prop-2-enamide), cysteine 145
• Biological source: Nesterenkonia sp. 10004
• Total number of polymer chains: 1
• Total formula weight: 30317.03

Authors

Kimani, S.W.,Sewell, B.T. (deposition date: 2013-01-30, release date: 2014-02-12, Last modification date: 2014-02-19)

• Primary citation: Kimani, S.W.,Hunter, R.,Vlok, M.,Watermeyer, J.,Sewell, B.T.; Covalent modifications of the active site cysteine occur as a result of mutating the glutamate of the catalytic triad in the amidase from Nesterenkonia sp.; To be Published,

Experimental method

X-RAY DIFFRACTION (1.4 Å)