1SKU
E. coli Aspartate Transcarbamylase 240's Loop Mutant (K244N)
Summary for 1SKU
Entry DOI | 10.2210/pdb1sku/pdb |
Related | 1EZZ 1FPB 1NBE |
Descriptor | Aspartate carbamoyltransferase catalytic chain, Aspartate carbamoyltransferase regulatory chain, MALONATE ION, ... (5 entities in total) |
Functional Keywords | allosteric enzyme, loop movements, small-angle x-ray scattering, domain closure, allosteric transition, intersubunit interactions, transferase |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 103266.22 |
Authors | Alam, N.,Stieglitz, K.A.,Caban, M.D.,Gourinath, S.,Tsuruta, H.,Kantrowitz, E.R. (deposition date: 2004-03-05, release date: 2004-03-30, Last modification date: 2023-08-23) |
Primary citation | Alam, N.,Stieglitz, K.A.,Caban, M.D.,Gourinath, S.,Tsuruta, H.,Kantrowitz, E.R. 240s Loop Interactions Stabilize the T State of Escherichia coli Aspartate Transcarbamoylase. J.Biol.Chem., 279:23302-23310, 2004 Cited by PubMed: 15014067DOI: 10.1074/jbc.M401637200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report