5wrn

X-ray diffraction
2.39Å resolution

Human thymidylate synthase complexed with dCMP

Released:
Source organism: Homo sapiens
Entry authors: Chen D, Nordlund P

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 289 amino acids
Theoretical weight: 33.17 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:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P43212
Unit cell:
a: 110.096Å b: 110.096Å c: 317.268Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.247
Expression system: Escherichia coli