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

Entry DOI	10.2210/pdb1mdr/pdb
Descriptor	MANDELATE RACEMASE, MAGNESIUM ION, ATROLACTIC ACID (2-PHENYL-LACTIC ACID), ... (4 entities in total)
Functional Keywords	racemase
Biological source	Pseudomonas putida
Total number of polymer chains	1
Total formula weight	38793.08
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: 2024-02-14)
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 Cited by PubMed: 8292591 DOI: 10.1021/bi00169a003 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation