› 3ly5

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
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-192636 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent RNA helicase DDX18 Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 29.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NVP1 (Residues: 149-387; Coverage: 36%)
Gene names: DDX18, cPERP-D
Sequence domains: DEAD/DEAH box helicase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand PO4 1 x PO4
Ligand MG 2 x MG
Ligand SCN 2 x SCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P31
Unit cell:
a: 41.34Å b: 41.34Å c: 230.541Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.246 0.274
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Dbp5, Gle1-IP6 and Nup159: a working model for mRNP export.
Folkmann et al. (2011)
15 more

4 mentions without citation

Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins.
Squeglia et al. (2020)
3 more