1Q95

Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate

Summary for 1Q95
DescriptorAspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (5 entities in total)
Functional Keywordsaspartate transcarbamylase, aspartate carbamoyltransferase, n-carbamyl-l-aspartate, pala, atcase-pala complex, r state, transferase
Biological sourceEscherichia coli
More
Total number of polymer chains12
Total formula weight310807.55
Authors
Huang, J.,Lipscomb, W.N. (deposition date: 2003-08-22, release date: 2004-06-08, Last modification date: 2011-07-13)
Primary citationHuang, J.,Lipscomb, W.N.
Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R-State Bound to PALA, or to Product Analogues Citrate and Phosphate
Biochemistry, 43:6415-6421, 2004
PubMed: 15157075
DOI: 110.1021/bi030213b
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.46 Å)
Structure validation
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178747

PDB entries from 2021-06-09