+Search query
-Structure paper
Title | 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. |
---|---|
Journal, issue, pages | To be Published |
Publish date | Jan 30, 2013 (structure data deposition date) |
Authors | Kimani, S.W. / Hunter, R. / Vlok, M. / Watermeyer, J. / Sewell, B.T. |
External links | Search PubMed |
Methods | X-ray diffraction |
Resolution | 1.4 - 1.92 Å |
Structure data | PDB-4izs: PDB-4izt: PDB-4izu: PDB-4izv: PDB-4izw: |
Chemicals | ChemComp-PEG: ChemComp-BMD: ChemComp-HOH: ChemComp-ACM: ChemComp-FTM: ChemComp-ROP: ChemComp-1HC: |
Source |
|
Keywords | HYDROLASE / butyramide / hydrolase/substrate / fluoroacetamide / acetamide / hydrolase-substrate complex / propionamide / acrylamide (prop-2-enamide) / cysteine 145 / active site |