Function and Biology Details
Reactions catalysed:
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
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
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Formamidopyrimidine-DNA glycosylase, catalytic domain
- DNA glycosylase/AP lyase, H2TH DNA-binding
- MutM-like, N-terminal
- Formamidopyrimidine-DNA glycosylase
- DNA glycosylase/AP lyase, zinc finger domain, DNA-binding site
- Zinc finger, FPG/IleRS-type
- Zinc finger, DNA glycosylase/AP lyase-type
- Small ribosomal subunit protein uS13-like, H2TH
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Formamidopyrimidine-DNA glycosylase and DNA (preferred)
PDBe Complex ID:
PDB-CPX-114059 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (3 distinct):
Formamidopyrimidine-DNA glycosylase
Molecule details ›
Chains: A, B, C, D
Length: 268 amino acids
Theoretical weight: 30.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 268 amino acids
Theoretical weight: 30.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P05523 (Residues: 2-269; Coverage: 100%)
Sequence domains:
- Formamidopyrimidine-DNA glycosylase N-terminal domain
- Formamidopyrimidine-DNA glycosylase H2TH domain
- Zinc finger found in FPG and IleRS
