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Showing results 1 to 11 of 11 for Uniprot_accession:P11444 - New search


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Method
Release date
Resolution (Å)
4m6u
P. putida mandelate racemase co-crystallized with tartronic acid x-ray diffraction 05/03/2014 1.8
4hnc
P. putida C92S/K166C/C264S mandelate racemase co-crystallized with benzilic acid x-ray diffraction 30/10/2013 1.889
4fp1
P. putida mandelate racemase co-crystallized with 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl) propionic acid x-ray diffraction 26/06/2013 1.68
3uxk
P. putida mandelate racemase co-crystallized with the intermediate analogue benzohydroxamate x-ray diffraction 08/02/2012 2.201
3uxl
P. putida mandelate racemase co-crystallized with the intermediate analogue cupferron x-ray diffraction 08/02/2012 2.201
1mdl
MANDELATE RACEMASE MUTANT K166R CO-CRYSTALLIZED WITH (R)-MANDELATE x-ray diffraction 14/10/1996 1.85
1dtn
MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE x-ray diffraction 14/10/1996 2.1
1mra
MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE x-ray diffraction 01/08/1996 2.1
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 x-ray diffraction 31/08/1994 2.1
2mnr
MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE. 2. CRYSTAL STRUCTURE OF MANDELATE RACEMASE AT 2.5 ANGSTROMS RESOLUTION: IDENTIFICATION OF THE ACTIVE SITE AND POSSIBLE CATALYTIC RESIDUES x-ray diffraction 31/01/1994 1.9
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 x-ray diffraction 31/10/1993 2.0
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