PDBe 2a1j

X-ray diffraction
2.7Å resolution

Crystal Structure of the Complex between the C-Terminal Domains of Human XPF and ERCC1

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA repair endonuclease XPF Chain: A
Molecule details ›
Chain: A
Length: 63 amino acids
Theoretical weight: 6.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92889 (Residues: 848-909; Coverage: 7%)
Gene names: ERCC11, ERCC4, XPF
Structure domains: 5' to 3' exonuclease, C-terminal subdomain
DNA excision repair protein ERCC-1 Chain: B
Molecule details ›
Chain: B
Length: 91 amino acids
Theoretical weight: 10.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07992 (Residues: 220-296; Coverage: 26%)
Gene name: ERCC1
Sequence domains: Helix-hairpin-helix motif
Structure domains: 5' to 3' exonuclease, C-terminal subdomain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3212
Unit cell:
a: 69.848Å b: 69.848Å c: 104.109Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.25 0.239 0.275
Expression system: Escherichia coli