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

Entry DOI	10.2210/pdb1acm/pdb
Descriptor	ASPARTATE CARBAMOYLTRANSFERASE, CATALYTIC CHAIN, ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (5 entities in total)
Functional Keywords	transferase (carbamoyl-p, aspartate)
Total number of polymer chains	4
Total formula weight	103288.14
Authors	Stevens, R.C.,Kantrowitz, E.R.,Lipscomb, W.N. (deposition date: 1992-07-08, release date: 1992-07-15, Last modification date: 2024-02-07)
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 Cited by PubMed: 1303763 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation