|Background:||The crystal structure of a periplasmic l-aspartate/l-glutamate binding protein (DEBP) from Shigella flexneri complexed with an l-glutamate molecule has been determined and refined to an atomic resolution of 1.0 A. There are two DEBP molecules in the asymmetric unit. The refined model contains 4462 non-hydrogen protein atoms, 730 water molecules, 2 bound glutamate molecules, and 2 Tris molecules from the buffer used in crystallization. The final R(cryst) and R(free) factors are 13.61% and 16.89%, respectively.|
|Protein Classification:||Transport protein|
|Structure Weight:||64851.95 Da|
|Molecule:||Periplasmic Binding Transport Protein|
|Chain Length:||287 amino acids|
|Ligand Chemical Component:||Glutamic acid; 2-amino-2-hydroxymethyl-propane-1,3-diol|
|Reference:||Hu, Y.L., Fan, C.-P., Fu, G.S., Zhu, D.Y., Jin, Q., Wang, D.-C. (2008) Crystal Structure of a Glutamate/Aspartate Binding Protein Complexed with a Glutamate Molecule: Structural Basis of Ligand Specificity at Atomic Resolution. J.Mol.Biol. 382: 99-111|
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