› 3qn2

X-ray diffraction
1.66Å resolution

Structure-based design of a disulfide-linked oligomeric form of the Simian Virus 40 (SV40) large T antigen DNA binding domain

Released:
DOI: 10.2210/pdb3qn2/pdb
PDB entry 3qn2 coloured by chain, front view.
PDB entry 3qn2 coloured by chain, side view.
PDB entry 3qn2 coloured by chain, top view.
Source organism: Macaca mulatta polyomavirus 1
Primary publication:
Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain.
Meinke G, Phelan P, Fradet-Turcotte A, Archambault J, Bullock PA
Acta Crystallogr D Biol Crystallogr 67 560-7 (2011)
PMID: 21636896

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136535 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Large T antigen Chain: A
Molecule details ›
Chain: A
Length: 134 amino acids
Theoretical weight: 15.33 KDa
Source organism: Macaca mulatta polyomavirus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: P03070 (Residues: 131-260; Coverage: 18%)
Sequence domains: Origin of replication binding protein
Structure domains: Replication Protein E1; Chain: A,

Ligands and Environments

1 bound ligand:
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P65
Unit cell:
a: 83.933Å b: 83.933Å c: 35.872Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.17 0.191
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The large tumor antigen: a "Swiss Army knife" protein possessing the functions required for the polyomavirus life cycle.
Topalis et al. (2013)
2 other articles

1 mention without citation

Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain.
Meinke et al. (2011)