› 1bnk

X-ray diffraction
2.7Å resolution

HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA

Released:
DOI: 10.2210/pdb1bnk/pdb
PDB entry 1bnk coloured by chain, front view.
PDB entry 1bnk coloured by chain, side view.
PDB entry 1bnk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision.
Lau AY, Schärer OD, Samson L, Verdine GL, Ellenberger T
Cell 95 249-58 (1998)
PMID: 9790531

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 domain:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-113497 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA-3-methyladenine glycosylase Chain: A
Molecule details ›
Chain: A
Length: 216 amino acids
Theoretical weight: 24.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P29372 (Residues: 80-295; Coverage: 73%)
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*YRRP*TP*TP*GP*CP*CP*T)-3') Chain: D
Molecule details ›
Chain: D
Length: 13 nucleotides
Theoretical weight: 3.83 KDa
Source organism: Homo sapiens
Expression system: Not provided
DNA (5'-D(*GP*GP*CP*AP*AP*TP*CP*AP*TP*GP*TP*CP*A)-3') Chain: E
Molecule details ›
Chain: E
Length: 13 nucleotides
Theoretical weight: 3.98 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 43.75Å b: 57.1Å c: 128.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.26
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

34 review citations

Base excision repair.
Krokan et al. (2013)
33 more

18 mentions without citation

AdoMet-dependent methylation, DNA methyltransferases and base flipping.
Cheng et al. (2001)
17 more