Structure of PDB 3i0w Chain A Binding Site BS01

Receptor Information
>3i0w Chain A (length=290) Species: 1488 (Clostridium acetobutylicum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDFDMIEEKKDSVIVRNVENFELKDIFDCGQCFRWHRQENGNYIGIAFEK
VVEVQKIGEDVVIYNINEEEFKNVWSEYFDLYRDYGEIKKELSRDPLLKK
SVDFGEGIRILRQDPFEILLSFIISANNRIPMIKKCINNISEKAGKKLEY
KGKIYYAFPTVDKLHEFTEKDFEECTAGFRAKYLKDTVDRIYNGELNLEY
IKSLNDNECHEELKKFMGVGPQVADCIMLFSMQKYSAFPVDTWVKKAMMS
LYVAPDVSLKKIRDFGREKFGSLSGFAQQYLFYYARENNI
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3i0w Structural basis for the lack of opposite base specificity of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase.
Resolution1.73 Å
Binding residue
(original residue number in PDB)		G30 S125 A126 N127 N128 R129 I130 F179 Y183 M217 G218 G220 P221 Q222 V223 P239 D241 T242 W243 K246 Q278 F282 R286
Binding residue
(residue number reindexed from 1)		G30 S125 A126 N127 N128 R129 I130 F179 Y183 M217 G218 G220 P221 Q222 V223 P239 D241 T242 W243 K246 Q278 F282 R286
Enzymatic activity
Catalytic site (original residue number in PDB) Q222 D241
Catalytic site (residue number reindexed from 1) Q222 D241
Enzyme Commision number 4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.
Gene Ontology
Molecular Function
GO:0003684 damaged DNA binding
GO:0003824 catalytic activity
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0140097 catalytic activity, acting on DNA
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006289 nucleotide-excision repair

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3i0w, PDBe:3i0w, PDBj:3i0w
PDBsum3i0w
PubMed19747886
UniProtQ97FM4

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