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-Structure paper
Title | Molecular mechanism of allosteric substrate activation in a thiamine diphosphate-dependent decarboxylase. |
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Journal, issue, pages | J. Biol. Chem., Vol. 282, Page 35269-35278, Year 2007 |
Publish date | Jun 1, 2007 (structure data deposition date) |
![]() | Versees, W. / Spaepen, S. / Wood, M.D. / Leeper, F.J. / Vanderleyden, J. / Steyaert, J. |
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Methods | X-ray diffraction |
Resolution | 1.85 - 3.2 Å |
Structure data | ![]() PDB-2q5j: ![]() PDB-2q5l: ![]() PDB-2q5o: ![]() PDB-2q5q: |
Chemicals | ![]() ChemComp-MG: ![]() ChemComp-TPW: ![]() ChemComp-HOH: ![]() ChemComp-CL: ![]() ChemComp-S1T: ![]() ChemComp-R1T: ![]() ChemComp-GOL: ![]() ChemComp-PPY: ![]() ChemComp-KPV: ![]() ChemComp-TLA: |
Source |
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![]() | LYASE / thiamine diphosphate / asymmetric dimer of dimers / open active site loops / cofactor analogue / open active site loop / covalent intermediate analogue / symmetrical dimer of dimers / closed active site loops / substrate complex |