› 3n5n

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb3n5n/pdb
PDB entry 3n5n coloured by chain, front view.
PDB entry 3n5n coloured by chain, side view.
PDB entry 3n5n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A structural hinge in eukaryotic MutY homologues mediates catalytic activity and Rad9-Rad1-Hus1 checkpoint complex interactions.
Luncsford PJ, Chang DY, Shi G, Bernstein J, Madabushi A, Patterson DN, Lu AL, Toth EA
J Mol Biol 403 351-70 (2010)
PMID: 20816984

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193782 (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:
Ligand SF4 2 x SF4
Ligand ACT 1 x ACT
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)

Quick links

Citations

6 review citations

Role of MUTYH in human cancer.
Mazzei et al. (2013)
5 more

16 mentions without citation

Emerging critical roles of Fe-S clusters in DNA replication and repair.
Fuss et al. (2015)
15 more