1D09
ASPARTATE TRANSCARBAMOYLASE COMPLEXED WITH N-PHOSPHONACETYL-L-ASPARTATE (PALA)
Summary for 1D09
Entry DOI | 10.2210/pdb1d09/pdb |
Related | 8ATC |
Descriptor | ASPARTATE CARBAMOYLTRANSFERASE CATALYTIC CHAIN, ASPARTATE CARBAMOYLTRANSFERASE REGULATORY CHAIN, N-(PHOSPHONACETYL)-L-ASPARTIC ACID, ... (5 entities in total) |
Functional Keywords | protein-inhibitor complex aspartate transcarbamoylase aspartate transcarbamylase, transferase |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 103602.52 |
Authors | Jin, L.,Stec, B.,Lipscomb, W.N.,Kantrowitz, E.R. (deposition date: 1999-09-09, release date: 2000-01-28, Last modification date: 2024-03-13) |
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 Cited by PubMed: 10651286DOI: 10.1002/(SICI)1097-0134(19991201)37:4<729::AID-PROT21>3.3.CO;2-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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