About: " Root mean square deviation in reference to starting structure (black) calculated between C? carbon coordinates of the first dimeric subunit versus the second subunit (intermonomer RMSD red) of the thymidylate synthase in function of time for 300 ns molecular dynamics simulation. Raise of the intermonomer RMSD value shows asymmetric unfolding of the subunits, especially in case of urea"

2TSR

Asymmetric Behavior of Thymidylate Synthase Dimer Subunits
in Denaturating Solvent Observed with Molecular Dynamics

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Details.

Scientist
Joana Trylska
Protein
thymidylate synthase enzyme
Ligand
GdmCl
Simulation Duration
300ns
InChIKey
N/A
SMILES
N/A
Molecular Formula
N/A
Protein Details
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH2 as the reductant
Ligand Details
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation.
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