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-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. |
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Journal, issue, pages | To be Published |
Publish date | Jan 30, 2013 (structure data deposition date) |
![]() | Kimani, S.W. / Hunter, R. / Vlok, M. / Watermeyer, J. / Sewell, B.T. |
![]() | 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 |
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![]() | HYDROLASE / butyramide / hydrolase/substrate / fluoroacetamide / acetamide / hydrolase-substrate complex / propionamide / acrylamide (prop-2-enamide) / cysteine 145 / active site |