Structure of PDB 3twm Chain B Binding Site BS01

Receptor Information
>3twm Chain B (length=261) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKT
IISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKWPSKYSKFFVELDDGL
ELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKK
ITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTS
IKEVIEKAVEVDADSSQFPSNWIFHNREKKPGKAFVDGKKIDFITAGGRT
TAYVPELQKLY
Ligand information
Receptor-Ligand Complex Structure
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PDB3twm Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine.
Resolution2.8 Å
Binding residue
(original residue number in PDB)
P2 E3 K60 G77 M78 R126 F128 G185 N186 R267 T268
Binding residue
(residue number reindexed from 1)
P1 E2 K59 G76 M77 R108 F110 G167 N168 R249 T250
Enzymatic activity
Catalytic site (original residue number in PDB) P2 E3
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.
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003684 damaged DNA binding
GO:0003906 DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0008270 zinc ion binding
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0019104 DNA N-glycosylase activity
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair

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Molecular Function

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Biological Process
External links
PDB RCSB:3twm, PDBe:3twm, PDBj:3twm
PDBsum3twm
PubMed22789755
UniProtO80358|FPG_ARATH Formamidopyrimidine-DNA glycosylase (Gene Name=FPG1)

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