1bj4
From Proteopedia
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RECOMBINANT SERINE HYDROXYMETHYLTRANSFERASE (HUMAN)
Overview
BACKGROUND: Serine hydroxymethyltransferase (SHMT) is a ubiquitous enzyme, found in all prokaryotes and eukaryotes. As an enzyme of the thymidylate, synthase metabolic cycle, SHMT catalyses the retro-aldol cleavage of, serine to glycine, with the resulting hydroxymethyl group being, transferred to tetrahydrofolate to form 5, 10-methylene-tetrahydrofolate., The latter is the major source of one-carbon units in metabolism. Elevated, SHMT activity has been shown to be coupled to the increased demand for DNA, synthesis in rapidly proliferating cells, particularly tumour cells., Consequently, the central role of SHMT in nucleotide biosynthesis makes it, an attractive target for cancer chemotherapy. RESULTS: We have solved the, crystal structure of human cytosolic SHMT by multiple isomorphous, ... [(full description)]
About this Structure
1BJ4 is a [Single protein] structure of sequence from [Homo sapiens] with PLP as [ligand]. Active as [[1]], with EC number [2.1.2.1]. Full crystallographic information is available from [OCA].
Reference
The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy., Renwick SB, Snell K, Baumann U, Structure. 1998 Sep 15;6(9):1105-16. PMID:9753690
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