› 1mun

X-ray diffraction
1.2Å resolution

CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI D138N MUTANT

Released:
DOI: 10.2210/pdb1mun/pdb
PDB 1mun coloured by chain and viewed from the front.
PDB 1mun coloured by chain and viewed from the side.
PDB 1mun coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily.
Guan Y, Manuel RC, Arvai AS, Parikh SS, Mol CD, Miller JH, Lloyd S, Tainer JA
Nat. Struct. Biol. 5 1058-64 (1998)
PMID: 9846876

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 domain:

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:
Ligand SF4 1 x SF4
Ligand IMD 5 x IMD
Ligand GOL 1 x GOL
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

Quick links

Citations

40 review citations

Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.
Banda et al. (2017)
39 more

3 mentions without citation

A graph-theory algorithm for rapid protein side-chain prediction.
Canutescu et al. (2003)
2 more