The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms
The structure was published by LeMagueres, P., Im, H., Dvorak, A., Strych, U., Benedik, M., and Krause, K.L., in 2003 in a paper entitled "Crystal structure at 1.45 A resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.45 Å and deposited in 2003.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of catabolic alanine racemase DadX. This molecule has the UniProt identifier Q9HTQ2 (ALR2_PSEAE). The sample contained 357 residues which is 100% of the natural sequence. Out of 357 residues 357 were observed and are deposited in the PDB.
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 most likely forms homodimers.
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: