3G5I

Crystal Structure of the E.coli RihA pyrimidine nucleosidase bound to a iminoribitol-based inhibitor

Summary for 3G5I

Entry DOI	10.2210/pdb3g5i/pdb
Related	1Q8F 1YOE
Descriptor	Pyrimidine-specific ribonucleoside hydrolase rihA, BETA-MERCAPTOETHANOL, CALCIUM ION, ... (5 entities in total)
Functional Keywords	open (alpha, beta) structure, glycosidase, hydrolase
Biological source	Escherichia coli
Total number of polymer chains	4
Total formula weight	136662.36
Authors	Garau, G.,Muzzolini, L.,Tornaghi, P.,Degano, M. (deposition date: 2009-02-05, release date: 2010-02-09, Last modification date: 2023-11-01)
Primary citation	Garau, G.,Muzzolini, L.,Tornaghi, P.,Degano, M. Active site plasticity revealed from the structure of the enterobacterial N-ribohydrolase RihA bound to a competitive inhibitor. Bmc Struct.Biol., 10:14-14, 2010 Cited by PubMed Abstract: Pyrimidine-preferring N-ribohydrolases (CU-NHs) are a class of Ca2+-dependent enzymes that catalyze the hydrolytic cleavage of the N-glycosidic bond in pyrimidine nucleosides. With the exception of few selected organisms, their physiological relevance in prokaryotes and eukaryotes is yet under investigation. PubMed: 20529317 DOI: 10.1186/1472-6807-10-14 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation