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-Structure paper
Title | Evolution of homo-oligomerization of methionine S-adenosyltransferases is replete with structure-function constrains. |
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Journal, issue, pages | Protein Sci., Vol. 31, Page e4352-e4352, Year 2022 |
Publish date | Feb 6, 2022 (structure data deposition date) |
![]() | Kleiner, D. / Shapiro Tuchman, Z. / Shmulevich, F. / Shahar, A. / Zarivach, R. / Kosloff, M. / Bershtein, S. |
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Methods | X-ray diffraction |
Resolution | 1.6 - 2.82 Å |
Structure data | ![]() PDB-7r2w: ![]() PDB-7r3b: |
Chemicals | ![]() ChemComp-ANP: ![]() ChemComp-MG: ![]() ChemComp-K: ![]() ChemComp-HOH: ![]() ChemComp-PHE: ![]() ChemComp-PPK: ![]() ChemComp-SAM: |
Source |
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![]() | TRANSFERASE / Dihedral D2 symmetry / homotetramer A4 symmetry / isologous interfaces 2 / S-adenosylmethionine synthetase |