Structure of PDB 1k82 Chain A

Receptor sequence
>1k82A (length=260) Species: 562 (Escherichia coli) [Search protein sequence]
PELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLS
VQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGK
VLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKK
TAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARV
IKAVLLRSIEQGGTTLKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQR
ATFYCRQCQK
3D structure
PDB1k82 Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) P1 E2
Catalytic site (residue number reindexed from 1) P1 E2
Enzyme Commision number 3.2.2.23: DNA-formamidopyrimidine glycosylase.
4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000703 oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0003684 damaged DNA binding
GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0004519 endonuclease activity
GO:0008270 zinc ion binding
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0016829 lyase activity
GO:0019104 DNA N-glycosylase activity
GO:0034039 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
GO:0046872 metal ion binding
GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease activity
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006974 DNA damage response
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1k82, PDBe:1k82, PDBj:1k82
PDBsum1k82
PubMed11912217
UniProtP05523|FPG_ECOLI Formamidopyrimidine-DNA glycosylase (Gene Name=mutM)

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