5L7V

Crystal Structure of BvGH123 with bond transition state analog Galthiazoline.

Summary for 5L7V

Entry DOI	10.2210/pdb5l7v/pdb
Descriptor	glycoside hydrolase, (3aR,5R,6R,7R,7aR)-5-(hydroxymethyl)-2-methyl-5,6,7,7a-tetrahydro-3aH-pyrano[3,2-d][1,3]thiazole-6,7-diol (3 entities in total)
Functional Keywords	tim barrel, bacon, hydrolase
Biological source	Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / NBRC 14291 / NCTC 11154)
Total number of polymer chains	2
Total formula weight	129403.02
Authors	Roth, C.,Petricevic, M.,John, A.,Goddard-Borger, E.D.,Davies, G.J.,Williams, S.J. (deposition date: 2016-06-03, release date: 2017-03-22, Last modification date: 2024-11-06)
Primary citation	Roth, C.,Petricevic, M.,John, A.,Goddard-Borger, E.D.,Davies, G.J.,Williams, S.J. Structural and mechanistic insights into a Bacteroides vulgatus retaining N-acetyl-beta-galactosaminidase that uses neighbouring group participation. Chem. Commun. (Camb.), 52:11096-11099, 2016 Cited by PubMed Abstract: Bacteroides vulgatus is a member of the human microbiota whose abundance is increased in patients with Crohn's disease. We show that a B. vulgatus glycoside hydrolase from the carbohydrate active enzyme family GH123, BvGH123, is an N-acetyl-β-galactosaminidase that acts with retention of stereochemistry, and, through a 3-D structure in complex with Gal-thiazoline, provide evidence in support of a neighbouring group participation mechanism. PubMed: 27546776 DOI: 10.1039/c6cc04649e PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.3 Å)

Structure validation