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-Structure paper
Title | Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes. |
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Journal, issue, pages | Biochemistry, Vol. 48, Page 1445-1453, Year 2009 |
Publish date | Apr 11, 2008 (structure data deposition date) |
Authors | Sakai, A. / Fedorov, A.A. / Fedorov, E.V. / Schnoes, A.M. / Glasner, M.E. / Brown, S. / Rutter, M.E. / Bain, K. / Chang, S. / Gheyi, T. ...Sakai, A. / Fedorov, A.A. / Fedorov, E.V. / Schnoes, A.M. / Glasner, M.E. / Brown, S. / Rutter, M.E. / Bain, K. / Chang, S. / Gheyi, T. / Sauder, J.M. / Burley, S.K. / Babbitt, P.C. / Almo, S.C. / Gerlt, J.A. |
External links | Biochemistry / PubMed:19220063 |
Methods | X-ray diffraction |
Resolution | 1.6 - 2 Å |
Structure data | PDB-3ct2: PDB-3dg3: PDB-3dg6: PDB-3dg7: PDB-3dgb: PDB-3fj4: |
Chemicals | ChemComp-MG: ChemComp-HOH: ChemComp-MUC: |
Source |
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Keywords | ISOMERASE / Structural genomics / target 9450f / MLE / PSI-2 / Protein Structure Initiative / New York SGX Research Center for Structural Genomics / NYSGXRC / muconate lactonizing enzyme / muconolactone binding / cis / cis-muconate |