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 undecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156730 (preferred)
Entry contents:
9 distinct polypeptide molecules
Macromolecules (9 distinct):
Non-homologous end-joining factor LIF1
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 28.67 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 246 amino acids
Theoretical weight: 28.67 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P53150 (Residues: 1-246; Coverage: 58%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
DNA ligase 4
Molecule details ›
Chain: C
Length: 264 amino acids
Theoretical weight: 30.37 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
Length: 264 amino acids
Theoretical weight: 30.37 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
- Canonical: Q08387 (Residues: 681-944; Coverage: 28%)
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
ESRF BEAMLINE ID13
Spacegroup:
P6422
Expression systems:
- Escherichia coli BL21
- Escherichia coli
