› 4xsd

X-ray diffraction
2.9Å resolution

Complex structure of thymidylate synthase from varicella zoster virus with a dUMP

Released:
DOI: 10.2210/pdb4xsd/pdb
PDB entry 4xsd coloured by chain, front view.
PDB entry 4xsd coloured by chain, side view.
PDB entry 4xsd coloured by chain, top view.
Source organism: Human herpesvirus 3 strain Oka vaccine
Primary publication:
Structure of the Varicella Zoster Virus Thymidylate Synthase Establishes Functional and Structural Similarities as the Human Enzyme and Potentiates Itself as a Target of Brivudine.
Hew K, Dahlroth SL, Veerappan S, Pan LX, Cornvik T, Nordlund P
PLoS One 10 e0143947 (2015)
PMID: 26630264

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-175585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 311 amino acids
Theoretical weight: 35.77 KDa
Source organism: Human herpesvirus 3 strain Oka vaccine
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4JQW2 (Residues: 8-295; Coverage: 96%)
Gene name: ORF13
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:
Ligand UMP 4 x UMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P32
Unit cell:
a: 150.17Å b: 150.17Å c: 89.16Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.242 0.24 0.28
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Dihydrofolate reductase, thymidylate synthase, and serine hydroxy methyltransferase: successful targets against some infectious diseases.
Shamshad et al. (2022)
5 other articles

2 mentions without citation

Distribution and effects of amino acid changes in drug-resistant α and β herpesviruses DNA polymerase.
Topalis et al. (2016)
1 more