1ACM

ARGININE 54 IN THE ACTIVE SITE OF ESCHERICHIA COLI ASPARTATE TRANSCARBAMOYLASE IS CRITICAL FOR CATALYSIS: A SITE-SPECIFIC MUTAGENESIS, NMR AND X-RAY CRYSTALLOGRAPHY STUDY

Summary for 1ACM

DescriptorASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN, ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (5 entities in total)
Functional Keywordstransferase (carbamoyl-p, aspartate)
Total number of polymer chains4
Total molecular weight103288.14
Authors
Stevens, R.C.,Kantrowitz, E.R.,Lipscomb, W.N. (deposition date: 1992-07-08, release date: 1992-07-15, Last modification date: 2017-11-29)
Primary citation
Stebbins, J.W.,Robertson, D.E.,Roberts, M.F.,Stevens, R.C.,Lipscomb, W.N.,Kantrowitz, E.R.
Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study.
Protein Sci., 1:1435-1446, 1992
PubMed: 1303763 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers81.3%9.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report