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-Structure paper
Title | Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase. |
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Journal, issue, pages | Biochemistry, Vol. 47, Page 9944-9954, Year 2008 |
Publish date | Aug 25, 2006 (structure data deposition date) |
![]() | Rakus, J.F. / Fedorov, A.A. / Fedorov, E.V. / Glasner, M.E. / Hubbard, B.K. / Delli, J.D. / Babbitt, P.C. / Almo, S.C. / Gerlt, J.A. |
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Methods | X-ray diffraction |
Resolution | 1.8 - 2.1 Å |
Structure data | ![]() PDB-2i5q: ![]() PDB-3box: ![]() PDB-3cxo: |
Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-MG: ![]() ChemComp-3LR: ![]() ChemComp-1N5: |
Source |
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![]() | LYASE / Enolase superfamily / Clone name 9265b1BCt1p1_10997_1 / Structural Genomics / PSI / Protein Structure Initiative / New York SGX Research Center for Structural Genomics / NYSGXRC / target 9265a / clone name 9265a2BSt6p1 / L-RHAMNONATE DEHYDRATASE / PSI-2 / 3-DEOXY-L-RHAMNONATE |