› 4hto

X-ray diffraction
2.81Å resolution

Crystal structure of the DBD domain of human DNA ligase IV Apo form

Released:
DOI: 10.2210/pdb4hto/pdb
PDB entry 4hto coloured by chain, front view.
PDB entry 4hto coloured by chain, side view.
PDB entry 4hto coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of DNA ligase IV-Artemis interaction in nonhomologous end-joining.
De Ioannes P, Malu S, Cortes P, Aggarwal AK
Cell Rep 2 1505-12 (2012)
PMID: 23219551

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase 4 Chain: A
Molecule details ›
Chain: A
Length: 240 amino acids
Theoretical weight: 27.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49917 (Residues: 1-240; Coverage: 26%)
Gene name: LIG4
Sequence domains: DNA ligase N terminus
Structure domains: DNA ligase, ATP-dependent, N-terminal domain

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C, NSLS BEAMLINE X6A
Spacegroup: F4132
Unit cell:
a: 196.236Å b: 196.236Å c: 196.236Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.259
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Non-homologous DNA end joining and alternative pathways to double-strand break repair.
Chang et al. (2017)
14 more

2 mentions without citation

Structural basis of DNA ligase IV-Artemis interaction in nonhomologous end-joining.
De Ioannes et al. (2012)
1 more