1USH

5'-NUCLEOTIDASE FROM E. COLI

Summary for 1USH

Entry DOI	10.2210/pdb1ush/pdb
Descriptor	5'-NUCLEOTIDASE, ZINC ION, CARBONATE ION, ... (5 entities in total)
Functional Keywords	5'-nucleotidase, udp-sugar hydrolase, phosphatase, hydrolase (phosphoric monoester), periplasmic protein, hydrolase
Biological source	Escherichia coli
Cellular location	Periplasm: P07024
Total number of polymer chains	1
Total formula weight	61469.85
Authors	Knofel, T.,Strater, N. (deposition date: 1998-09-16, release date: 1999-06-15, Last modification date: 2024-10-16)
Primary citation	Knofel, T.,Strater, N. X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site. Nat.Struct.Biol., 6:448-453, 1999 Cited by PubMed Abstract: The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system. PubMed: 10331872 DOI: 10.1038/8253 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.73 Å)

Structure validation