1sx8

X-ray diffraction
2.15Å resolution

EcoRV bound to cognate DNA and Mn2+

Released:
Source organism: Escherichia coli
Primary publication:
DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites.
Biochemistry 43 6841-57 (2004)
PMID: 15170321

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)
PDBe Complex ID:
PDB-CPX-114619 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Type II restriction enzyme EcoRV Chains: A, B
Molecule details ›
Chains: A, B
Length: 244 amino acids
Theoretical weight: 28.5 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04390 (Residues: 2-245; Coverage: 100%)
Gene name: ecoRVR
Sequence domains: Restriction endonuclease EcoRV
Structure domains: DNA mismatch repair MutH/Restriction endonuclease, type II
5'-D(*C*AP*AP*GP*AP*TP*AP*TP*CP*TP*T)-3' Chains: C, D
Molecule details ›
Chains: C, D
Length: 11 nucleotides
Theoretical weight: 3.33 KDa
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 47.8Å b: 49.1Å c: 63.7Å
α: 96.9° β: 108.9° γ: 107.1°
R-values:
R R work R free
0.213 0.213 0.254
Expression systems:
  • Escherichia coli
  • Not provided