PDBe 3ii6

X-ray diffraction
2.4Å resolution

Structure of human Xrcc4 in complex with the tandem BRCT domains of DNA LigaseIV.

Released:

Function and Biology Details

Reaction catalysed:
(1a) ATP + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA repair protein XRCC4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 203 amino acids
Theoretical weight: 23.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13426 (Residues: 1-203; Coverage: 60%)
Gene name: XRCC4
Structure domains:
DNA ligase 4 Chains: X, Y
Molecule details ›
Chains: X, Y
Length: 263 amino acids
Theoretical weight: 30.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49917 (Residues: 654-911; Coverage: 28%)
Gene name: LIG4
Sequence domains:
Structure domains: BRCT domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P1
Unit cell:
a: 67.243Å b: 85.982Å c: 111.608Å
α: 67.34° β: 82.86° γ: 74.52°
R-values:
R R work R free
0.24 0.24 0.28
Expression system: Escherichia coli