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 domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
DNA ligase 3 (preferred)
PDBe Complex ID:
PDB-CPX-156087 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase 3
Molecule details ›
Chain: A
Length: 88 amino acids
Theoretical weight: 9.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: DNA ligase 3 BRCT domain
Structure domains: BRCT domain
Length: 88 amino acids
Theoretical weight: 9.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P49916 (Residues: 924-1009; Coverage: 9%)
Sequence domains: DNA ligase 3 BRCT domain
Structure domains: BRCT domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
distance geometry, simulated annealing, torsion angle dynamics
Expression system: Escherichia coli
