› 3ed7

X-ray diffraction
1.56Å resolution

Replacement of Val3 in Human Thymidylate Synthase Affects Its Kinetic Properties and Intracellular Stability

Released:
DOI: 10.2210/pdb3ed7/pdb
PDB entry 3ed7 coloured by chain, front view.
PDB entry 3ed7 coloured by chain, side view.
PDB entry 3ed7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Replacement of Val3 in human thymidylate synthase affects its kinetic properties and intracellular stability .
Huang X, Gibson LM, Bell BJ, Lovelace LL, Peña MM, Berger FG, Berger SH, Lebioda L
Biochemistry 49 2475-82 (2010)
PMID: 20151707

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-138196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 33.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04818 (Residues: 26-313; Coverage: 92%)
Gene names: OK/SW-cl.29, TS, TYMS
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 95.546Å b: 95.546Å c: 80.923Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.209 0.233
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential.
Zhao et al. (2021)
5 other articles

3 mentions without citation

Crystal structure of mouse thymidylate synthase in tertiary complex with dUMP and raltitrexed reveals N-terminus architecture and two different active site conformations.
Dowierciał et al. (2014)
2 more