1s68

X-ray diffraction
1.9Å resolution

Structure and Mechanism of RNA Ligase

Released:
Source organism: Escherichia virus T4
Primary publication:
Structure and mechanism of RNA ligase.
Structure 12 327-39 (2004)
PMID: 14962393

Function and Biology Details

Reaction catalysed:
(1a) ATP + [RNA ligase]-L-lysine = [RNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152250 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA ligase 2 Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 28.33 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P32277 (Residues: 1-249; Coverage: 75%)
Gene names: 24.1, Y10A
Sequence domains: RNA ligase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200, NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 57.717Å b: 89.892Å c: 47.737Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.227
Expression system: Escherichia coli BL21(DE3)