1ZA2
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution
Summary for 1ZA2
Entry DOI | 10.2210/pdb1za2/pdb |
Related | 1TU0 1ZA1 |
Descriptor | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, SODIUM ION, ... (7 entities in total) |
Functional Keywords | ordered substrate binding, cooperativity, transferase |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 104645.66 |
Authors | Wang, J.,Stieglitz, K.A.,Cardia, J.P.,Kantrowitz, E.R. (deposition date: 2005-04-05, release date: 2005-06-07, Last modification date: 2023-08-23) |
Primary citation | Wang, J.,Stieglitz, K.A.,Cardia, J.P.,Kantrowitz, E.R. Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase Proc.Natl.Acad.Sci.Usa, 102:8881-8886, 2005 Cited by PubMed: 15951418DOI: 10.1073/pnas.0503742102 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report