› 1ypv

X-ray diffraction
1.8Å resolution

Structure of human thymidylate synthase at low salt conditions

Released:
DOI: 10.2210/pdb1ypv/pdb
PDB entry 1ypv coloured by chain, front view.
PDB entry 1ypv coloured by chain, side view.
PDB entry 1ypv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human thymidylate synthase under low-salt conditions.
Lovelace LL, Minor W, Lebioda L
Acta Crystallogr D Biol Crystallogr 61 622-7 (2005)
PMID: 15858273

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: 313 amino acids
Theoretical weight: 36.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04818 (Residues: 1-313; Coverage: 100%)
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 PO4 2 x PO4
2 modified residues:
Ligand SCH 1 x SCH
Ligand CME 3 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3121
Unit cell:
a: 95.772Å b: 95.772Å c: 81.851Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.226 0.226 0.244
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states.
Chen et al. (2017)
7 more

12 mentions without citation

Protein-protein interface-binding peptides inhibit the cancer therapy target human thymidylate synthase.
Cardinale et al. (2011)
11 more