› 4ez8

X-ray diffraction
1.17Å resolution

Crystal structure of mouse thymidylate sythase in ternary complex with N(4)-hydroxy-2'-deoxycytidine-5'-monophosphate and the cofactor product, dihydrofolate

Released:
DOI: 10.2210/pdb4ez8/pdb
PDB entry 4ez8 coloured by chain, front view.
PDB entry 4ez8 coloured by chain, side view.
PDB entry 4ez8 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structures of complexes of mouse thymidylate synthase crystallized with N4-OH-dCMP alone or in the presence of N5,10-methylenetetrahydrofolate
Dowiercial A, Jarmula A, Rypniewski W, Wilk P, Kierdaszuk B, Banaszak K, Gorecka K, Rode W
Pteridines (2013)

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139660 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 35 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07607 (Residues: 1-307; Coverage: 100%)
Gene name: Tyms
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

3 bound ligands:
Ligand NOH 1 x NOH
Ligand DHF 1 x DHF
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 71.121Å b: 112.045Å c: 88.297Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.108 0.107 0.13
Expression system: Escherichia coli

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