› 3llm

X-ray diffraction
2.8Å resolution

Crystal Structure Analysis of a RNA Helicase

Released:
DOI: 10.2210/pdb3llm/pdb
PDB entry 3llm coloured by chain, front view.
PDB entry 3llm coloured by chain, side view.
PDB entry 3llm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human RNA helicase A (DHX9): structural basis for unselective nucleotide base binding in a DEAD-box variant protein.
Schütz P, Wahlberg E, Karlberg T, Hammarström M, Collins R, Flores A, Schüler H
J Mol Biol 400 768-82 (2010)
PMID: 20510246

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent RNA helicase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 235 amino acids
Theoretical weight: 26.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08211 (Residues: 329-563; Coverage: 19%)
Gene names: DDX9, DHX9, LKP, NDH2
Sequence domains: DEAD/DEAH box helicase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

4 bound ligands:
Ligand MN 2 x MN
Ligand CAC 1 x CAC
Ligand ADP 2 x ADP
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P3221
Unit cell:
a: 113.7Å b: 113.7Å c: 141.65Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.211 0.238
Expression system: Escherichia coli

Quick links

Citations

3 review citations

DExD/H-box RNA helicases as mediators of anti-viral innate immunity and essential host factors for viral replication.
Fullam et al. (2013)
2 more

3 mentions without citation

Roles of individual domains in the function of DHX29, an essential factor required for translation of structured mammalian mRNAs.
Dhote et al. (2012)
2 more