Structure of PDB 3twm Chain A Binding Site BS02

Receptor Information

>3twm Chain A (length=261) Species: 3702 (Arabidopsis thaliana)

PELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKT
IISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKWPSKYSKFFVELDDGL
ELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKK
ITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTS
IKEVIEKAVEVDADSSQFPSNWIFHNREKKPGKAFVDGKKIDFITAGGRT
TAYVPELQKLY

Ligand information

>3twm Chain D (length=15)

tggtagacgtggacg

Receptor-Ligand Complex Structure

Structure summary

• 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): K33 Y107 K125 R126 R127 F128 K168 T170
• Binding residue (residue number reindexed from 1): K32 Y89 K107 R108 R109 F110 K150 T152

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

External links

• PDB: RCSB:3twm, PDBe:3twm, PDBj:3twm
• PDBsum: 3twm
• PubMed: 22789755
• UniProt: O80358|FPG_ARATH Formamidopyrimidine-DNA glycosylase (Gene Name=FPG1)