1kg3

X-ray diffraction
1.55Å resolution

Crystal structure of the core fragment of MutY from E.coli at 1.55A resolution

Released:
Source organism: Escherichia coli
Entry authors: Gilboa R, Kilshtein A, Zharkov DO, Kycia JH, Gerchman SE, Grollman AP, Shoham G

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148180 (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: Escherichia coli
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: NSLS BEAMLINE X26C
Spacegroup: C2
Unit cell:
a: 84.45Å b: 50.2Å c: 70.5Å
α: 90° β: 123.29° γ: 90°
R-values:
R R work R free
0.172 0.172 0.228
Expression system: Escherichia coli