› 1az3

X-ray diffraction
2.4Å resolution

ECORV ENDONUCLEASE, UNLIGANDED, FORM B

Released:
DOI: 10.2210/pdb1az3/pdb
PDB entry 1az3 coloured by chain, front view.
PDB entry 1az3 coloured by chain, side view.
PDB entry 1az3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis.
Perona JJ, Martin AM
J Mol Biol 273 207-25 (1997)
PMID: 9367757

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137618 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type II restriction enzyme EcoRV Chains: A, B
Molecule details ›
Chains: A, B
Length: 244 amino acids
Theoretical weight: 28.56 KDa
Source organism: 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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 73.7Å b: 122.8Å c: 59.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.315

Quick links

Citations

2 review citations

Structure and function of type II restriction endonucleases.
Pingoud et al. (2001)
1 more

2 mentions without citation

The energetic contribution of induced electrostatic asymmetry to DNA bending by a site-specific protein.
Hancock et al. (2011)
1 more