5ZMY

Crystal structure of a cis-epoxysuccinate hydrolase producing D(-)-tartaric acids

Summary for 5ZMY

• Entry DOI: 10.2210/pdb5zmy/pdb
• Related: 5ZMU
• Descriptor: Cis-epoxysuccinate hydrolase, ZINC ION, D(-)-TARTARIC ACID, ... (4 entities in total)
• Functional Keywords: zn-binding, tim-barrel, hydrolase
• Biological source: Bordetella sp. BK-52
• Total number of polymer chains: 8
• Total formula weight: 278909.00

Authors

Dong, S.,Liu, X.,Wang, X.,Feng, Y. (deposition date: 2018-04-06, release date: 2018-08-08, Last modification date: 2023-11-22)

Primary citation

Dong, S.,Liu, X.,Cui, G.Z.,Cui, Q.,Wang, X.,Feng, Y.
Structural insight into the catalytic mechanism of a cis-epoxysuccinate hydrolase producing enantiomerically pure d(-)-tartaric acid.
Chem. Commun. (Camb.), 54:8482-8485, 2018

PubMed Abstract: Crystal structure determination and mutagenesis analysis of a cis-epoxysuccinate hydrolase which produces enantiomerically pure d(-)-tartaric acids revealed a zinc ion and essential residues in the stereoselective mechanism for the catalytic reaction of the small mirror symmetric substrate.

PubMed: 30003205
DOI: 10.1039/c8cc04398a

Experimental method

X-RAY DIFFRACTION (1.87 Å)