› 4q0r

X-ray diffraction
2.75Å resolution

The catalytic core of Rad2 (complex I)

Released:
DOI: 10.2210/pdb4q0r/pdb
PDB entry 4q0r coloured by chain, front view.
PDB entry 4q0r coloured by chain, side view.
PDB entry 4q0r coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.
Miętus M, Nowak E, Jaciuk M, Kustosz P, Studnicka J, Nowotny M
Nucleic Acids Res 42 10762-75 (2014)
PMID: 25120270

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-117999 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
DNA repair protein RAD2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 367 amino acids
Theoretical weight: 43.02 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07276 (Residues: 2-986; Coverage: 35%)
Gene names: RAD2, YGR258C
Sequence domains:
DNA (5'-D(*CP*TP*GP*AP*GP*TP*CP*AP*GP*AP*GP*CP*AP*AP*A)-3') Chain: D
Molecule details ›
Chain: D
Length: 15 nucleotides
Theoretical weight: 4.63 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 26 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P3221
Unit cell:
a: 94.085Å b: 94.085Å c: 155.264Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.248 0.245 0.31
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

5 review citations

XPA: A key scaffold for human nucleotide excision repair.
Sugitani et al. (2016)
4 more

1 mention without citation

Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.
Miętus et al. (2014)