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-Structure paper
| Title | Rhizobium etli has two L-asparaginases with low sequence identity but similar structure and catalytic center. |
|---|---|
| Journal, issue, pages | Acta Crystallogr D Struct Biol, Vol. 79, Page 775-791, Year 2023 |
| Publish date | Feb 17, 2023 (structure data deposition date) |
Authors | Loch, J.I. / Worsztynowicz, P. / Sliwiak, J. / Grzechowiak, M. / Imiolczyk, B. / Pokrywka, K. / Chwastyk, M. / Gilski, M. / Jaskolski, M. |
External links | Acta Crystallogr D Struct Biol / PubMed:37494066 |
| Methods | X-ray diffraction |
| Resolution | 1.3 - 2.503 Å |
| Structure data | ![]() PDB-8cly: ![]() PDB-8clz: ![]() PDB-8col: ![]() PDB-8ori: ![]() PDB-8osw: |
| Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-CL: ![]() ChemComp-EDO: ![]() ChemComp-HOH: ![]() ChemComp-MG: ![]() ChemComp-PEG: ![]() ChemComp-PGE: |
| Source |
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Keywords | HYDROLASE / amidohydrolase / zinc binding protein / structural homology / enzymatic mechanism / enzyme kinetics / occluded water molecules / L-asparaginase / Rhizobium etli / enzyme |
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rhizobium etli (bacteria)
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