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

Entry DOI	10.2210/pdb1q95/pdb
Descriptor	Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (5 entities in total)
Functional Keywords	aspartate transcarbamylase, aspartate carbamoyltransferase, n-carbamyl-l-aspartate, pala, atcase-pala complex, r state, transferase
Biological source	Escherichia coli More
Total number of polymer chains	12
Total formula weight	310807.55
Authors	Huang, J.,Lipscomb, W.N. (deposition date: 2003-08-22, release date: 2004-06-08, Last modification date: 2023-08-16)
Primary citation	Huang, 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 Cited by PubMed: 15157075 DOI: 10.1021/bi030213b PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.46 Å)

Structure validation