› 3qi5

X-ray diffraction
2.2Å resolution

Crystal structure of human alkyladenine DNA glycosylase in complex with 3,N4-ethenocystosine containing duplex DNA

Released:
DOI: 10.2210/pdb3qi5/pdb
PDB entry 3qi5 coloured by chain, front view.
PDB entry 3qi5 coloured by chain, side view.
PDB entry 3qi5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the inhibition of human alkyladenine DNA glycosylase (AAG) by 3,N4-ethenocytosine-containing DNA.
Lingaraju GM, Davis CA, Setser JW, Samson LD, Drennan CL
J Biol Chem 286 13205-13 (2011)
PMID: 21349833

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-116768 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA-3-methyladenine glycosylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 24.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29372 (Residues: 84-298; Coverage: 72%)
Gene names: AAG, ANPG, MID1, MPG
Sequence domains: Methylpurine-DNA glycosylase (MPG)
Structure domains: Methylpurine-DNA glycosylase (MPG)
DNA (5'-D(*GP*AP*CP*AP*TP*GP*(EDC)P*TP*TP*GP*CP*CP*T)-3') Chains: C, E
Molecule details ›
Chains: C, E
Length: 13 nucleotides
Theoretical weight: 3.97 KDa
Source organism: Homo sapiens
Expression system: Not provided
DNA (5'-D(*GP*GP*CP*AP*AP*GP*CP*AP*TP*GP*TP*CP*A)-3') Chains: D, F
Molecule details ›
Chains: D, F
Length: 13 nucleotides
Theoretical weight: 4 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand MN 2 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P1
Unit cell:
a: 41.226Å b: 41.22Å c: 82.144Å
α: 81.23° β: 88.4° γ: 89.15°
R-values:
R R work R free
0.239 0.236 0.284
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Regulation of DNA Alkylation Damage Repair: Lessons and Therapeutic Opportunities.
Soll et al. (2017)
12 other articles

5 mentions without citation

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