3WMR

Crystal structure of VinJ

Summary for 3WMR

Entry DOI	10.2210/pdb3wmr/pdb
Descriptor	Proline iminopeptidase, GLYCEROL, 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE, ... (4 entities in total)
Functional Keywords	alpha/beta hydrolase fold, hydrolase
Biological source	Streptomyces halstedii
Total number of polymer chains	3
Total formula weight	107710.79
Authors	Shinohara, Y.,Miyanaga, A.,Kudo, F.,Eguchi, T. (deposition date: 2013-11-22, release date: 2014-02-05, Last modification date: 2023-11-08)
Primary citation	Shinohara, Y.,Miyanaga, A.,Kudo, F.,Eguchi, T. The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates Febs Lett., 588:995-1000, 2014 Cited by PubMed Abstract: VinJ is an amidohydrolase belonging to the serine peptidase family that catalyzes the hydrolysis of the terminal aminoacyl moiety of a polyketide intermediate during the biosynthesis of vicenistatin. Herein, we report the crystal structure of VinJ. VinJ possesses a unique hydrophobic tunnel for the recognition of the polyketide chain moiety of its substrate in the cap domain. Taken together with the results of phylogenetic analysis, our results suggest that VinJ represents a new amidohydrolase family that is different from the known α/β hydrolase type serine peptidases. PubMed: 24530530 DOI: 10.1016/j.febslet.2014.01.060 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation