PDBe 1oyw

X-ray diffraction
1.8Å resolution

Structure of the RecQ Catalytic Core

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: 59.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P15043 (Residues: 1-522; Coverage: 86%)
Gene names: JW5855, b3822, recQ
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 66.696Å b: 54.589Å c: 78.83Å
α: 90° β: 110.85° γ: 90°
R-values:
R R work R free
0.213 0.193 0.245
Expression system: Escherichia coli