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Structure paper

TitleOptimal alignment for enzymatic proton transfer: Structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 100, Page 50-55, Year 2003
Publish dateDec 12, 2002 (structure data deposition date)
AuthorsJogl, G. / Rozovsky, S. / McDermott, A.E. / Tong, L.
External linksProc. Natl. Acad. Sci. USA / PubMed:12509510
MethodsX-ray diffraction
Resolution1.2 - 1.6 Å
Structure data

PDB-1ney:
Triosephosphate Isomerase in Complex with DHAP
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-1nf0:
Triosephosphate Isomerase in Complex with DHAP
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-13P:
1,3-DIHYDROXYACETONEPHOSPHATE

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsISOMERASE / yeast / triosephosphate isomerase / DHAP / dihydroxyacetone phosphate / michaelis complex

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