2IPO
E. coli Aspartate Transcarbamoylase complexed with N-phosphonacetyl-L-asparagine
Summary for 2IPO
Entry DOI | 10.2210/pdb2ipo/pdb |
Related | 1D09 2IQE |
Descriptor | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, N~2~-(PHOSPHONOACETYL)-L-ASPARAGINE, ... (7 entities in total) |
Functional Keywords | aspartate transcarbamoylase, allosteric, inhibitor design, domain closure, transferase |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 104069.04 |
Authors | Cardia, J.P.,Eldo, J.,Xia, J.,O'Day, E.M.,Tsuruta, H.,Kantrowitz, E.R. (deposition date: 2006-10-12, release date: 2007-08-28, Last modification date: 2023-08-30) |
Primary citation | Cardia, J.P.,Eldo, J.,Xia, J.,O'Day, E.M.,Tsuruta, H.,Gryncel, K.R.,Kantrowitz, E.R. Use of L-asparagine and N-phosphonacetyl-L-asparagine to investigate the linkage of catalysis and homotropic cooperativity in E. coli aspartate transcarbomoylase. Proteins, 71:1088-1096, 2008 Cited by PubMed: 18004787DOI: 10.1002/prot.21760 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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