Structure of PDB 3twm Chain B Binding Site BS01
Receptor Information
>3twm Chain B (length=261) Species:
3702
(Arabidopsis thaliana) [
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PELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKT
IISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKWPSKYSKFFVELDDGL
ELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKK
ITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTS
IKEVIEKAVEVDADSSQFPSNWIFHNREKKPGKAFVDGKKIDFITAGGRT
TAYVPELQKLY
Ligand information
>3twm Chain E (length=16) [
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agcgtccacgtctacc
Receptor-Ligand Complex Structure
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PDB
3twm
Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine.
Resolution
2.8 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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:3twm
,
PDBe:3twm
,
PDBj:3twm
PDBsum
3twm
PubMed
22789755
UniProt
O80358
|FPG_ARATH Formamidopyrimidine-DNA glycosylase (Gene Name=FPG1)
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