1MDR

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

Summary for 1MDR

DescriptorMANDELATE RACEMASE, MAGNESIUM ION, ATROLACTIC ACID (2-PHENYL-LACTIC ACID), ... (4 entities in total)
Functional Keywordsracemase
Biological sourcePseudomonas putida
Total number of polymer chains1
Total molecular weight38793.08
Authors
Landro, J.A.,Gerlt, J.A.,Kozarich, J.W.,Koo, C.W.,Shah, V.J.,Kenyon, G.L.,Neidhart, D.J.,Fujita, S.,Petsko, G.A. (deposition date: 1993-11-19, release date: 1994-08-31, Last modification date: 2017-11-29)
Primary citation
Landro, J.A.,Gerlt, J.A.,Kozarich, J.W.,Koo, C.W.,Shah, V.J.,Kenyon, G.L.,Neidhart, D.J.
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.
Biochemistry, 33:635-643, 1994
PubMed: 8292591 (PDB entries with the same primary citation)
DOI: 10.1021/bi00169a003
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
?

Structure validation

ClashscoreRamachandran outliersSidechain outliers302.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload