› 6oju

X-ray diffraction
2.88Å resolution

Crystal structure of human thymidylate synthase Delta (7-29) in complex with dUMP and 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-D-glutamic acid

Released:
DOI: 10.2210/pdb6oju/pdb
PDB entry 6oju coloured by chain, front view.
PDB entry 6oju coloured by chain, side view.
PDB entry 6oju coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Understanding the structural basis of species selective, stereospecific inhibition for Cryptosporidium and human thymidylate synthase.
Czyzyk DJ, Valhondo M, Jorgensen WL, Anderson KS
FEBS Lett 593 2069-2078 (2019)
PMID: 31172516

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138193 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 290 amino acids
Theoretical weight: 33.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04818 (Residues: 1-313; Coverage: 93%)
Gene names: OK/SW-cl.29, TS, TYMS
Sequence domains: Thymidylate synthase

Ligands and Environments

2 bound ligands:
Ligand UMP 4 x UMP
Ligand D96 4 x D96
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 62.097Å b: 124.853Å c: 80.364Å
α: 90° β: 92.12° γ: 90°
R-values:
R R work R free
0.215 0.213 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Chiral evasion and stereospecific antifolate resistance in Staphylococcus aureus.
Wang et al. (2022)
1 more

1 mention without citation

Understanding the structural basis of species selective, stereospecific inhibition for Cryptosporidium and human thymidylate synthase.
Czyzyk et al. (2019)