1kqj

X-ray diffraction
1.7Å resolution

Crystal Structure of a Mutant of MutY Catalytic Domain

Released:
Source organism: Escherichia coli
Entry authors: Messick TE, Chmiel NH, Golinelli MP, David SS, Joshua-Tor L

Function and Biology Details

Reaction catalysed:
Hydrolyzes free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenine DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 25.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P17802 (Residues: 1-225; Coverage: 64%)
Gene names: JW2928, b2961, micA, mutY
Sequence domains: HhH-GPD superfamily base excision DNA repair protein
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: C2
Unit cell:
a: 83.55Å b: 49.9Å c: 71.01Å
α: 90° β: 122.56° γ: 90°
R-values:
R R work R free
0.191 0.191 0.208
Expression system: Escherichia coli