2L5H

Solution Structure of the H189Q mutant of the Enzyme I dimer Using Residual Dipolar Couplings and Small Angle X-Ray Scattering

Summary for 2L5H

Related2HWG 3EZA 2WQD 2HRO 2KX9 2XDF
DescriptorPhosphoenolpyruvate-protein phosphotransferase (1 entity in total)
Functional Keywordsprotein, dimer, transferase
Biological sourceEscherichia coli
Cellular locationCytoplasm P08839
Total number of polymer chains2
Total molecular weight126818.66
Authors
Takayama, Y.D.,Schwieters, C.D.,Grishaev, A.,Guirlando, R.,Clore, G. (deposition date: 2010-11-01, release date: 2011-01-12, Last modification date: 2012-04-25)
Primary citation
Takayama, Y.,Schwieters, C.D.,Grishaev, A.,Ghirlando, R.,Clore, G.M.
Combined Use of Residual Dipolar Couplings and Solution X-ray Scattering To Rapidly Probe Rigid-Body Conformational Transitions in a Non-phosphorylatable Active-Site Mutant of the 128 kDa Enzyme I Dimer.
J.Am.Chem.Soc., 133:424-427, 2011
PubMed: 21162528 (PDB entries with the same primary citation)
DOI: 10.1021/ja109866w
MImport into Mendeley
Experimental method
SOLUTION NMR
SOLUTION SCATTERING
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers481.3%17.7%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures