PDBe 3vnn

X-ray diffraction
2.9Å resolution

Crystal Structure of a sub-domain of the nucleotidyltransferase (adenylation) domain of human DNA ligase IV

Released:

Function and Biology Details

Reaction catalysed:
ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase 4 Chain: A
Molecule details ›
Chain: A
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%)
Gene name: LIG4
Structure domains: DNA ligase/mRNA capping enzyme

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P4122
Unit cell:
a: 39.086Å b: 39.086Å c: 197.393Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.277 0.273 0.305
Expression system: Escherichia coli