4V3B

The structure of alpha2,3-sialyltransferase variant 1 from Pasteurella dagmatis in complex with the donor product CMP

Summary for 4V3B

Entry DOI	10.2210/pdb4v3b/pdb
Related	4V2U 4V38 4V39 4V3C
Descriptor	SIALYLTRANSFERASE, CYTIDINE-5'-MONOPHOSPHATE (3 entities in total)
Functional Keywords	transferase
Biological source	PASTEURELLA DAGMATIS
Total number of polymer chains	1
Total formula weight	46026.25
Authors	Pavkov-Keller, T.,Schmoelzer, K.,Czabany, T.,Luley-Goedl, C.,Ribitsch, D.,Schwab, H.,Nidetzky, B.,Gruber, K. (deposition date: 2014-10-17, release date: 2015-04-08, Last modification date: 2024-01-10)
Primary citation	Schmoelzer, K.,Czabany, T.,Pavkov-Keller, T.,Luley-Goedl, C.,Ribitsch, D.,Schwab, H.,Gruber, K.,Nidetzky, B. Complete Switch from Alpha2,3- to Alpha2,6-Regioselectivity in Pasteurella Dagmatis Beta-D-Galactoside Sialyltransferase by Active-Site Redesign Chem.Commun.(Camb.), 51:3083-, 2015 Cited by PubMed Abstract: Structure-guided active-site redesign of a family GT-80 β-D-galactoside sialyltransferase (from Pasteurella dagmatis) to change enzyme regioselectivity from α-2,3 in the wild type to α-2,6 in a P7H-M117A double mutant is reported. Biochemical data for sialylation of lactose together with protein crystal structures demonstrate highly precise enzyme engineering. PubMed: 25619424 DOI: 10.1039/C4CC09772F PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.18 Å)

Structure validation