1CM2

STRUCTURE OF HIS15ASP HPR AFTER HYDROLYSIS OF RINGED SPECIES.

Summary for 1CM2

Related1CM3
DescriptorHISTIDINE-CONTAINING PROTEIN (2 entities in total)
Functional Keywordsphosphotransferase, succinimide, isoimide, transferase
Biological sourceEscherichia coli
Cellular locationCytoplasm P0AA04
Total number of polymer chains1
Total molecular weight9106.27
Authors
Napper, S.,Delbaere, L.T.J.,Waygood, E.B. (deposition date: 1999-05-13, release date: 2000-05-17, Last modification date: 2011-07-13)
Primary citation
Napper, S.,Delbaere, L.T.,Waygood, E.B.
The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization
J.Biol.Chem., 274:21776-21782, 1999
PubMed: 10419492 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.274.31.21776
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers120 5.7%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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171588
PDB entries from 2020-11-25