Function and Biology Details
Reaction catalysed:
(1a) ATP + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assemblies composition:
Assembly name:
DNA repair protein XRCC1 and DNA ligase 3 (preferred)
PDBe Complex ID:
PDB-CPX-156088 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA repair protein XRCC1
Molecule details ›
Chains: A, B
Length: 98 amino acids
Theoretical weight: 11.75 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: BRCT domain, a BRCA1 C-terminus domain
Structure domains: BRCT domain
Length: 98 amino acids
Theoretical weight: 11.75 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q60596 (Residues: 534-631; Coverage: 16%)
Sequence domains: BRCT domain, a BRCA1 C-terminus domain
Structure domains: BRCT domain
DNA ligase 3
Molecule details ›
Chains: C, D
Length: 88 amino acids
Theoretical weight: 9.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: DNA ligase 3 BRCT domain
Structure domains: BRCT domain
Length: 88 amino acids
Theoretical weight: 9.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P49916 (Residues: 924-1008; Coverage: 8%)
Sequence domains: DNA ligase 3 BRCT domain
Structure domains: BRCT domain
