Structure of PDB 3twm Chain B

Receptor sequence
>3twmB (length=261) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
PELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKT
IISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKWPSKYSKFFVELDDGL
ELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKK
ITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTS
IKEVIEKAVEVDADSSQFPSNWIFHNREKKPGKAFVDGKKIDFITAGGRT
TAYVPELQKLY
3D structure
PDB3twm Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine.
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 dna B P2 E3 K60 G77 M78 R126 F128 G185 N186 R267 T268 P1 E2 K59 G76 M77 R108 F110 G167 N168 R249 T250
BS02 dna B K33 Y107 K125 R126 R127 F128 K167 I169 K32 Y89 K107 R108 R109 F110 K149 I151
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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