1ZA1
Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP at 2.20 A resolution
Summary for 1ZA1
Entry DOI | 10.2210/pdb1za1/pdb |
Related | 1NBE 1ZA2 |
Descriptor | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, ZINC ION, ... (5 entities in total) |
Functional Keywords | ordered substrate binding, cooperativity, transferase |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 104058.59 |
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 (2.2 Å) |
Structure validation
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