› 1pvs

X-ray diffraction
2.4Å resolution

3-methyladenine Glcosylase II(AlkA) Hypoxanthine complex

Released:
DOI: 10.2210/pdb1pvs/pdb
PDB entry 1pvs coloured by chain, front view.
PDB entry 1pvs coloured by chain, side view.
PDB entry 1pvs coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
3-methyladenine-DNA glycosylase II: the crystal structure of an AlkA-hypoxanthine complex suggests the possibility of product inhibition.
Teale M, Symersky J, DeLucas L
Bioconjug Chem 13 403-7
PMID: 12009927

Function and Biology Details

Reaction catalysed: 
Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-3-methyladenine glycosylase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 282 amino acids
Theoretical weight: 31.43 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04395 (Residues: 1-282; Coverage: 100%)
Gene names: JW2053, aidA, alkA, b2068
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 7HP 2 x 7HP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 58.005Å b: 75.979Å c: 61.417Å
α: 90° β: 110.03° γ: 90°
R-values:
R R work R free
0.232 0.232 0.292
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Computational comparison of the stacking interactions between the aromatic amino acids and the natural or (cationic) methylated nucleobases.
Rutledge et al. (2008)
2 more

3 mentions without citation

Recent advances in the structural mechanisms of DNA glycosylases.
Brooks et al. (2013)
2 more