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: 15014067 DOI: 10.1074/jbc.M401637200 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation