Crystal structure of biosynthetic alaine racemase in D-cycloserine-bound form from Escherichia coli
The structure was published by Wu, D., Hu, T., Zhang, L., et al., Ding, J., Jiang, H., and Shen, X., in 2008 in a paper entitled "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" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Alanine racemase.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: