1CB0

STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE AT 1.7 A RESOLUTION

Summary for 1CB0

Entry DOI	10.2210/pdb1cb0/pdb
Descriptor	PROTEIN (5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE), ADENINE (3 entities in total)
Functional Keywords	methylthioadenosine phosphorylase, purine nucleoside phosphorylase, purine salvage, adenine, transferase
Biological source	Homo sapiens (human)
Total number of polymer chains	1
Total formula weight	31412.18
Authors	Appleby, T.C.,Erion, M.D.,Ealick, S.E. (deposition date: 1999-02-26, release date: 1999-07-05, Last modification date: 2023-12-27)
Primary citation	Appleby, T.C.,Erion, M.D.,Ealick, S.E. The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis. Structure Fold.Des., 7:629-641, 1999 Cited by PubMed Abstract: 5'-Deoxy-5'-methylthioadenosine phosphorylase (MTAP) catalyzes the reversible phosphorolysis of 5'-deoxy-5'-methylthioadenosine (MTA) to adenine and 5-methylthio-D-ribose-1-phosphate. MTA is a by-product of polyamine biosynthesis, which is essential for cell growth and proliferation. This salvage reaction is the principle source of free adenine in human cells. Because of its importance in coupling the purine salvage pathway to polyamine biosynthesis MTAP is a potential chemotherapeutic target. PubMed: 10404592 DOI: 10.1016/S0969-2126(99)80084-7 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation