PDBe 3uby

X-ray diffraction
2Å resolution

Crystal structure of human alklyadenine DNA glycosylase in a lower and higher-affinity complex with DNA

Released:

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 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: 3-methyladenine DNA Glycosylase; Chain A
DNA (5'-D(*GP*AP*CP*AP*TP*GP*(EDC)P*TP*TP*GP*CP*CP*T)-3') Chains: C, D
Molecule details ›
Chains: C, D
Length: 13 nucleotides
Theoretical weight: 3.97 KDa
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: P43
Unit cell:
a: 41.168Å b: 41.168Å c: 262.546Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.219 0.265
Expression systems:
  • Escherichia coli
  • Not provided