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 ligase 3
Molecule details ›
Chains: A, C
Length: 89 amino acids
Theoretical weight: 10.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: DNA ligase 3 BRCT domain
Structure domains: BRCT domain
Length: 89 amino acids
Theoretical weight: 10.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P49916 (Residues: 924-1008; Coverage: 8%)
Sequence domains: DNA ligase 3 BRCT domain
Structure domains: BRCT domain
DNA repair protein XRCC1
Molecule details ›
Chains: B, D
Length: 106 amino acids
Theoretical weight: 12.63 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: BRCT domain, a BRCA1 C-terminus domain
Structure domains: BRCT domain
Length: 106 amino acids
Theoretical weight: 12.63 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q60596 (Residues: 531-631; Coverage: 16%)
Sequence domains: BRCT domain, a BRCA1 C-terminus domain
Structure domains: BRCT domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-007 HF
Spacegroup:
P212121
Expression system: Escherichia coli BL21
