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This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.

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spinqualitylabelsall models PDB ID 1hvy Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1hvy, resolution 1.90Å ()
Ligands:	, ,
Non-Standard Residues:
Activity:	Thymidylate synthase, with EC number 2.1.1.45
Structural annotation: Resources: CATH : 1Hvya00, 1Hvyb00, 1Hvyc00, 1Hvyd00 InterPro : Ipr020940, Ipr000398, Ipr023451 Pfam : PF00303 SCOP : d1hvya_, d1hvyb_, d1hvyc_, d1hvyd_
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Thymidylate Synthase

Thymidylate Synthase is a protein found in all organisms that make DNA. Thymidylate Synthase (TS) is the essential enzyme that catalyzes the formation of dTMP from dUMP, using 5,10-methylenetetrahydrofolate (mTHF) as a cosubstrate.Human thymidylate synthase is in the closed conformation when complexed with dUMP and raltitrexed, an antifolate drug.^[1] Wikipedia

Overview

Thymidylate Synthase catalyzes the reductive methylation of deoxyuridylic acid during the de novo synthesis of thymidylic acid (Jenh et al., 1985). This reaction occurs primarily during the S phase of the cell cycle. TS is an essential enzyme in proliferating cells that are not supplied with an alternate source of thymidine nucleotides. Research has shown tat TS enzyme levels are much higher in rapidly proliferating cells than in non dividing cells (Jenh et al., 1985).

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