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4IZV

The E41Q/C145A double mutant of the amidase from Nesterenkonia sp. AN1 in complex with acrylamide

Summary for 4IZV
Entry DOI10.2210/pdb4izv/pdb
Related3HKX 4IZS 4IZT 4IZU 4IZW
DescriptorAmidase, PROPIONAMIDE, prop-2-enamide, ... (4 entities in total)
Functional Keywordshydrolase, active site, acrylamide (prop-2-enamide), cysteine 145, hydrolase-substrate complex, hydrolase/substrate
Biological sourceNesterenkonia sp. 10004
Total number of polymer chains1
Total formula weight30282.95
Authors
Kimani, S.W.,Sewell, B.T. (deposition date: 2013-01-30, release date: 2014-02-12, Last modification date: 2024-11-20)
Primary citationKimani, 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 (1.65 Å)
Structure validation

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