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X-ray diffraction
2.67Å resolution

Human Thymidylate Synthase Stabilized in Active Conformation by R163K Mutation: Asymmetry and Reactivity of Cys195

Released:
DOI: 10.2210/pdb2rda/pdb
PDB entry 2rda coloured by chain, front view.
PDB entry 2rda coloured by chain, side view.
PDB entry 2rda coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The R163K mutant of human thymidylate synthase is stabilized in an active conformation: structural asymmetry and reactivity of cysteine 195.
Gibson LM, Lovelace LL, Lebioda L
Biochemistry 47 4636-43 (2008)
PMID: 18370400

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 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 313 amino acids
Theoretical weight: 35.73 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

2 bound ligands:
Ligand PO4 5 x PO4
Ligand BME 2 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 123.794Å b: 123.794Å c: 284.766Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.209 0.279
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

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

5 mentions without citation

The R163K mutant of human thymidylate synthase is stabilized in an active conformation: structural asymmetry and reactivity of cysteine 195.
Gibson et al. (2008)
4 more