4IZV
The E41Q/C145A double mutant of the amidase from Nesterenkonia sp. AN1 in complex with acrylamide
Summary for 4IZV
Entry DOI | 10.2210/pdb4izv/pdb |
Related | 3HKX 4IZS 4IZT 4IZU 4IZW |
Descriptor | Amidase, PROPIONAMIDE, prop-2-enamide, ... (4 entities in total) |
Functional Keywords | hydrolase, active site, acrylamide (prop-2-enamide), cysteine 145, hydrolase-substrate complex, hydrolase/substrate |
Biological source | Nesterenkonia sp. 10004 |
Total number of polymer chains | 1 |
Total formula weight | 30282.95 |
Authors | |
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 (1.65 Å) |
Structure validation
Download full validation report