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:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
DNA ligase 4 (preferred)
PDBe Complex ID:
PDB-CPX-156091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase 4
Molecule details ›
Chain: A
Length: 139 amino acids
Theoretical weight: 16.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: ATP dependent DNA ligase domain
Structure domains: DNA ligase/mRNA capping enzyme
Length: 139 amino acids
Theoretical weight: 16.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P49917 (Residues: 268-406; Coverage: 15%)
Sequence domains: ATP dependent DNA ligase domain
Structure domains: DNA ligase/mRNA capping enzyme
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-1
Spacegroup:
P4122
Expression system: Escherichia coli
