› 4lh6

X-ray diffraction
1.65Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) NAD(+) + [DNA ligase]-L-lysine = [DNA ligase]-N(6)-(5'-adenylyl)-L-lysine + beta-nicotinamide D-nucleotide
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA ligase Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 36.86 KDa
Source organism: Enterococcus faecalis V583
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q837V6 (Residues: 1-323; Coverage: 48%)
Gene names: EF_0722, ligA
Sequence domains: NAD-dependent DNA ligase adenylation domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand 1X7 1 x 1X7
Ligand NMN 1 x NMN
Ligand ACT 1 x ACT
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2221
Unit cell:
a: 48.955Å b: 104.377Å c: 136.709Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.219 0.248
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Biochemical and Structural Characterisation of DNA Ligases from Bacteria and Archaea.
Pergolizzi et al. (2016)
3 more

1 mention without citation

Structure and two-metal mechanism of a eukaryal nick-sealing RNA ligase.
Unciuleac et al. (2015)