› 5lb8

X-ray diffraction
3.4Å resolution

Crystal structure of human RECQL5 helicase APO form.

Released:
DOI: 10.2210/pdb5lb8/pdb
PDB entry 5lb8 coloured by chain, front view.
PDB entry 5lb8 coloured by chain, side view.
PDB entry 5lb8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5.
Newman JA, Aitkenhead H, Savitsky P, Gileadi O
Nucleic Acids Res 45 4231-4243 (2017)
PMID: 28100692

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent DNA helicase Q5 Chains: A, D
Molecule details ›
Chains: A, D
Length: 518 amino acids
Theoretical weight: 57.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O94762 (Residues: 11-526; Coverage: 52%)
Gene names: RECQ5, RECQL5
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P43212
Unit cell:
a: 68.74Å b: 68.74Å c: 396.307Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.302 0.301 0.322
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

RecQ and Fe-S helicases have unique roles in DNA metabolism dictated by their unwinding directionality, substrate specificity, and protein interactions.
Estep et al. (2018)
5 more

4 mentions without citation

New Insights Into DNA Helicases as Druggable Targets for Cancer Therapy.
Datta et al. (2018)
3 more