1BJ4

RECOMBINANT SERINE HYDROXYMETHYLTRANSFERASE (HUMAN)

Summary for 1BJ4

Entry DOI	10.2210/pdb1bj4/pdb
Descriptor	Serine hydroxymethyltransferase, cytosolic, PYRIDOXAL-5'-PHOSPHATE (3 entities in total)
Functional Keywords	transferase, metabolic role, pyridoxal 5'-phosphate
Biological source	Homo sapiens (human)
Cellular location	Cytoplasm: P34896
Total number of polymer chains	1
Total formula weight	51971.00
Authors	Renwick, S.B.,Snell, K. (deposition date: 1998-07-02, release date: 1999-08-16, Last modification date: 2023-02-08)
Primary citation	Renwick, S.B.,Snell, K.,Baumann, U. The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy Structure, 6:1105-1116, 1998 Cited by PubMed Abstract: 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. PubMed: 9753690 DOI: 10.1016/S0969-2126(98)00112-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.65 Å)

Structure validation