PDBe 3n5n

X-ray diffraction
2.3Å resolution

Crystal structure analysis of the catalytic domain and interdomain connector of human MutY homologue

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenine DNA glycosylase Chains: X, Y
Molecule details ›
Chains: X, Y
Length: 287 amino acids
Theoretical weight: 31.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UIF7 (Residues: 76-362; Coverage: 53%)
Gene names: MUTYH, MYH
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P21
Unit cell:
a: 60.311Å b: 82.167Å c: 63.46Å
α: 90° β: 100.9° γ: 90°
R-values:
R R work R free
0.208 0.206 0.251
Expression system: Escherichia coli BL21(DE3)