2vbj

X-ray diffraction
1.95Å resolution

Molecular basis of human XPC gene recognition and cleavage by engineered homing endonuclease heterodimers

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-507195 (preferred)
Entry contents:
2 distinct polypeptide molecules
2 distinct DNA molecules
Macromolecules (4 distinct):
DNA endonuclease I-CreI Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 17.57 KDa
Source organism: Chlamydomonas reinhardtii
Expression system: Escherichia coli
UniProt:
  • Canonical: P05725 (Residues: 2-153; Coverage: 93%)
Sequence domains: LAGLIDADG endonuclease
Structure domains: Homing endonucleases
DNA endonuclease I-CreI Chain: B
Molecule details ›
Chain: B
Length: 152 amino acids
Theoretical weight: 17.45 KDa
Source organism: Chlamydomonas reinhardtii
Expression system: Escherichia coli
UniProt:
  • Canonical: P05725 (Residues: 2-153; Coverage: 93%)
Sequence domains: LAGLIDADG endonuclease
Structure domains: Homing endonucleases
5'-D(*TP*CP*TP*GP*CP*CP*TP*TP*TP*TP *TP*TP*GP*AP*AP*GP*GP*AP*TP*CP*CP*TP*AP*A)-3' Chain: C
Molecule details ›
Chain: C
Length: 24 nucleotides
Theoretical weight: 7.33 KDa
5'-D(*TP*TP*AP*GP*GP*AP*TP*CP*CP*TP *TP*CP*AP*AP*AP*AP*AP*AP*GP*GP*CP*AP*GP*A)-3' Chain: E
Molecule details ›
Chain: E
Length: 24 nucleotides
Theoretical weight: 7.41 KDa

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 44.552Å b: 68.7Å c: 88.731Å
α: 90° β: 95.36° γ: 90°
R-values:
R R work R free
0.15 0.147 0.216
Expression system: Escherichia coli