ON THE ROLE OF LYSINE 166 IN THE MECHANISM OF MANDELATE RACEMASE FROM PSEUDOMONAS PUTIDA: MECHANISTIC AND CRYSTALLOGRAPHIC EVIDENCE FOR STEREOSPECIFIC ALKYLATION BY (R)-ALPHA-PHENYLGLYCIDATE
The structure was published by Landro, J.A., Gerlt, J.A., Kozarich, J.W., et al., Neidhart, D.J., Fujita, S., and Petsko, G.A., in 1994 in a paper entitled "The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1993.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of MANDELATE RACEMASE. This molecule has the UniProt identifier P11444 (MANR_PSEPU). The sample contained 357 residues which is 99% 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 homooctamers.
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: