5lst

X-ray diffraction
2.75Å resolution

Crystal structure of the human RecQL4 helicase.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent DNA helicase Q4 Chain: A
Molecule details ›
Chain: A
Length: 693 amino acids
Theoretical weight: 76.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O94761 (Residues: 427-1116; Coverage: 57%)
Gene names: RECQ4, RECQL4
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3121
Unit cell:
a: 131.001Å b: 131.001Å c: 96.344Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.183 0.231
Expression system: Escherichia coli BL21(DE3)