1D09

ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)

Summary for 1D09

Related8ATC
DescriptorASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN, ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (5 entities in total)
Functional Keywordsprotein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase, transferase
Biological sourceEscherichia coli
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Total number of polymer chains4
Total molecular weight103602.52
Authors
Jin, L.,Stec, B.,Lipscomb, W.N.,Kantrowitz, E.R. (deposition date: 1999-09-09, release date: 2000-01-28, Last modification date: 2011-07-13)
Primary citation
Jin, L.,Stec, B.,Lipscomb, W.N.,Kantrowitz, E.R.
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A.
Proteins, 37:729-742, 1999
PubMed: 10651286 (PDB entries with the same primary citation)
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<729::AID-PROT21>3.3.CO;2-6
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers182.1%7.5%6.8%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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