Crystal structure of biosynthetic alaine racemase in D-cycloserine-bound form from Escherichia coli

Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis

0.1M HEPES, 1.6M ammonium sulfate, pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

This is a twinned structure, the detwin fraction is 0.400, and operator is 'h, -h-k, -l'.

alpha/beta barrel, Cell shape, Cell wall biogenesis/degradation, Isomerase, Peptidoglycan synthesis, Pyridoxal phosphate