1MNS
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
Summary for 1MNS
Entry DOI | 10.2210/pdb1mns/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 | 38574.80 |
Authors | Neidhart, D.J.,Landro, J.A.,Kozarich, J.W. (deposition date: 1993-07-06, release date: 1993-10-31, Last modification date: 2024-06-05) |
Primary citation | 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. 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: 8292591DOI: 10.1021/bi00169a003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report