› 3fe2

X-ray diffraction
2.6Å resolution

Human DEAD-BOX RNA helicase DDX5 (P68), conserved domain I in complex with ADP

Released:
DOI: 10.2210/pdb3fe2/pdb
PDB entry 3fe2 coloured by chain, front view.
PDB entry 3fe2 coloured by chain, side view.
PDB entry 3fe2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparative structural analysis of human DEAD-box RNA helicases.
Schütz P, Karlberg T, van den Berg S, Collins R, Lehtiö L, Högbom M, Holmberg-Schiavone L, Tempel W, Park HW, Hammarström M, Moche M, Thorsell AG, Schüler H
PLoS One 5 (2010)
PMID: 20941364

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-148187 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable ATP-dependent RNA helicase DDX5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 242 amino acids
Theoretical weight: 27.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17844 (Residues: 68-307; Coverage: 39%)
Gene names: DDX5, G17P1, HELR, HLR1
Sequence domains: DEAD/DEAH box helicase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand SO4 3 x SO4
Ligand ADP 2 x ADP
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2221
Unit cell:
a: 84.57Å b: 106.87Å c: 117.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.273
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

10 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)
9 more