1oyy

X-ray diffraction
2.5Å resolution

Structure of the RecQ Catalytic Core bound to ATP-gamma-S

Released:
Source organism: Escherichia coli
Primary publication:
High-resolution structure of the E.coli RecQ helicase catalytic core.
EMBO J. 22 4910-21 (2003)
PMID: 14517231

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent DNA helicase RecQ Chain: A
Molecule details ›
Chain: A
Length: 523 amino acids
Theoretical weight: 58.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P15043 (Residues: 1-523; Coverage: 86%)
Gene names: JW5855, b3822, recQ
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 66.591Å b: 54.534Å c: 78.686Å
α: 90° β: 110.78° γ: 90°
R-values:
R R work R free
0.21 0.21 0.298
Expression system: Escherichia coli