1enj

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME FROM BACTERIOPHAGE T4: REFINEMENT AT 1.45 ANGSTROMS AND X-RAY ANALYSIS OF THE THREE ACTIVE SITE MUTANTS

Released:

Function and Biology Details

Reactions catalysed:
Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endonuclease V Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 16.1 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
UniProt:
  • Canonical: P04418 (Residues: 1-138; Coverage: 100%)
Sequence domains: Pyrimidine dimer DNA glycosylase
Structure domains: T4 endonuclease V

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 41.4Å b: 40.1Å c: 37.4Å
α: 90° β: 90.35° γ: 90°
R-values:
R R work R free
0.221 not available not available
Expression system: Not provided