PDBe 3a42

X-ray diffraction
2.6Å resolution

Crystal structure of MvNei1

Released:

Function and Biology Details

Reactions catalysed:
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. 
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable formamidopyrimidine-DNA glycosylase Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.58 KDa
Source organism: Acanthamoeba polyphaga mimivirus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5UQ00 (Residues: 1-287; Coverage: 100%)
Gene name: MIMI_L315
Sequence domains:
Structure domains: N-terminal domain of MutM-like DNA repair proteins

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P65
Unit cell:
a: 123.241Å b: 123.241Å c: 44.849Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.209 0.268
Expression system: Escherichia coli