4ATD

Crystal structure of native Raucaffricine glucosidase

Summary for 4ATD

Entry DOI	10.2210/pdb4atd/pdb
Related	4A3Y
Descriptor	RAUCAFFRICINE-O-BETA-D-GLUCOSIDASE, SULFATE ION (3 entities in total)
Functional Keywords	alkaloid, hydrolase
Biological source	RAUVOLFIA SERPENTINA (SERPENTWOOD)
Total number of polymer chains	2
Total formula weight	116144.99
Authors	Xia, L.,Rajendran, C.,Ruppert, M.,Panjikar, S.,Wang, M.,Stoeckigt, J. (deposition date: 2012-05-05, release date: 2013-01-16, Last modification date: 2023-12-20)
Primary citation	Xia, L.,Rajendran, C.,Ruppert, M.,Panjikar, S.,Wang, M.,Stoeckigt, J. High Speed X-Ray Analysis of Plant Enzymes at Room Temperature Phytochemistry, 91:88-, 2013 Cited by PubMed Abstract: X-ray measurements at room temperature (295 K) deliver high quality data sets with unprecedented speed (<2 min), as shown for crystallized raucaffricine-O-β-D-glucosidase (RG), its mutant RG-Glu186Gln and several ligand complexes of the enzyme which participates in alkaloid biosynthesis in the plant Rauvolfia. The data obtained are compared with data sets measured under typical cryo conditions (100K). Under both conditions, density maps are highly comparable and favor the described protocol for room temperature measurements, potentially paving the way for future crystallographic studies capturing biosynthetic pathway intermediates. PubMed: 22704651 DOI: 10.1016/J.PHYTOCHEM.2012.05.009 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation