PDBe 1b96

X-ray diffraction
2.3Å resolution

ANALYSIS OF A MUTATIONAL HOT-SPOT IN THE ECORV RESTRICTION ENDONUCLEASE: A CATALYTIC ROLE FOR A MAIN CHAIN CARBONYL GROUP

Released:

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
RESTRICTION ENDONUCLEASE ECORV Chains: A, B
Molecule details ›
Chains: A, B
Length: 244 amino acids
Theoretical weight: 28.56 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
Structure domains: DNA mismatch repair MutH/Restriction endonuclease, type II
DNA (5'-D(*AP*AP*AP*GP*AP*TP*AP*TP*CP*TP*T)-3') Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 nucleotides
Theoretical weight: 3.36 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P1
Unit cell:
a: 48.35Å b: 48.78Å c: 63.64Å
α: 96.61° β: 108.94° γ: 107.44°
R-values:
R R work R free
0.189 0.189 0.282
Expression systems:
  • Escherichia coli
  • Not provided