Function and Biology Details
Reaction catalysed:
(1a) ATP + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
DNA ligase IV complex (preferred)
PDBe Complex ID:
PDB-CPX-156092 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA repair protein XRCC4
Molecule details ›
Chains: A, B
Length: 213 amino acids
Theoretical weight: 24.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: DNA double-strand break repair and V(D)J recombination protein XRCC4
Structure domains:
Length: 213 amino acids
Theoretical weight: 24.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q13426 (Residues: 1-213; Coverage: 63%)
Sequence domains: DNA double-strand break repair and V(D)J recombination protein XRCC4
Structure domains:
DNA ligase 4
Molecule details ›
Chain: C
Length: 37 amino acids
Theoretical weight: 4.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: DNA ligase IV
Length: 37 amino acids
Theoretical weight: 4.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P49917 (Residues: 748-784; Coverage: 4%)
Sequence domains: DNA ligase IV
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-4
Spacegroup:
P212121
Expression system: Escherichia coli BL21(DE3)
