1mun

X-ray diffraction
1.2Å resolution

CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT

Released:

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenine DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 25.05 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P17802 (Residues: 1-225; Coverage: 64%)
Gene names: JW2928, b2961, micA, mutY
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 82.5Å b: 49Å c: 69.4Å
α: 90° β: 122.9° γ: 90°
R-values:
R R work R free
0.124 not available 0.169
Expression system: Not provided