Literature summary for 2.1.1.45 extracted from

Dowiercial, A.; Wilk, P.; Rypniewski, W.; Rode, W.; Jarmula, A.
Crystal structure of mouse thymidylate synthase in tertiary complex with dUMP and raltitrexed reveals N-terminus architecture and two different active site conformations (2014), BioMed Res. Int., 2014, 945803.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with substrate dUMP and antifolate inhibitor raltitrexed, to 1.74 A resolution.The structure reveals a well-ordered segment of 13 N-terminal amino acids, whose ordered conformation is stabilized due to specific crystal packing.The structure consists of two homodimers, differing in conformation, one being more closed (dimer AB) and thus supporting tighter binding of ligands, and the other being more open (dimer CD) and thus allowing weaker binding of ligands. Conformational changes lead to a ligand-induced closing of the active site cleft	Mus musculus

Crystallization (Comment)

Organism

in complex with substrate dUMP and antifolate inhibitor raltitrexed, to 1.74 A resolution.The structure reveals a well-ordered segment of 13 N-terminal amino acids, whose ordered conformation is stabilized due to specific crystal packing.The structure consists of two homodimers, differing in conformation, one being more closed (dimer AB) and thus supporting tighter binding of ligands, and the other being more open (dimer CD) and thus allowing weaker binding of ligands. Conformational changes lead to a ligand-induced closing of the active site cleft

Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P07607	-	-

Synonyms

Synonyms	Comment	Organism
TYMS	-	Mus musculus

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Release 2023.1 (January 2023)