PDBe 1b04

X-ray diffraction
2.8Å resolution

STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE

Released:

Function and Biology Details

Reaction catalysed:
NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 318 amino acids
Theoretical weight: 35.83 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O87703 (Residues: 1-318; Coverage: 48%)
Gene names: lig, ligA
Sequence domains: NAD-dependent DNA ligase adenylation domain
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P43212
Unit cell:
a: 95.72Å b: 95.72Å c: 225.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.23 0.31
Expression system: Escherichia coli BL21