3pc7

X-ray diffraction
1.65Å resolution

X-ray crystal structure of the DNA ligase III-alpha BRCT domain.

Released:

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 88 amino acids
Theoretical weight: 10 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49916 (Residues: 924-1009; Coverage: 9%)
Gene name: LIG3
Sequence domains: DNA ligase 3 BRCT domain
Structure domains: BRCT domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P43212
Unit cell:
a: 70.13Å b: 70.13Å c: 62.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.143 0.14 0.198
Expression system: Escherichia coli BL21(DE3)