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X-ray diffraction
2.4Å resolution

STRUCTURE OF MUTANT (E165H) OF THE HSDR SUBUNIT OF THE ECOR124I RESTRICTION ENZYME IN COMPLEX WITH ATP

Released:
Source organism: Escherichia coli
Entry authors: Baikova T, Stsiapanava A, Moche M, Degtjarik O, Kuta-Smatanova I, Ettrich R

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates, ATP is simultaneously hydrolyzed.
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type I restriction enzyme EcoR124II R protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 1038 amino acids
Theoretical weight: 120.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P10486 (Residues: 1-1032; Coverage: 100%)
Gene names: hsdR, hsr
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 85.221Å b: 124.542Å c: 128.54Å
α: 90° β: 107.77° γ: 90°
R-values:
R R work R free
0.21 0.208 0.244
Expression system: Escherichia coli BL21(DE3)