1TUG
Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5-Prime-Triphosphate (CTP)
Summary for 1TUG
Entry DOI | 10.2210/pdb1tug/pdb |
Related | 1NBE 1TTH 1TU0 3AT1 |
Descriptor | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, MALONATE ION, ... (7 entities in total) |
Functional Keywords | protein structure-function, site specific mutagenesis, domain closure, allosteric transition, hydrolase-hydrolase regulator complex, hydrolase/hydrolase regulator |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 104424.71 |
Authors | Stieglitz, K.,Stec, B.,Baker, D.P.,Kantrowitz, E.R. (deposition date: 2004-06-24, release date: 2004-07-20, Last modification date: 2024-04-03) |
Primary citation | Stieglitz, K.,Stec, B.,Baker, D.P.,Kantrowitz, E.R. Monitoring the Transition from the T to the R State in E.coli Aspartate Transcarbamoylase by X-ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States. J.Mol.Biol., 341:853-868, 2004 Cited by PubMed: 15288791DOI: 10.1016/j.jmb.2004.06.002 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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