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: 1303763PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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