Structure of PDB 3g0q Chain A

Receptor sequence
>3g0qA (length=344) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
PAREFQRDLLDWFARERRDLPWRKDRDPYKVWVSEVMLQQTRVETVIPYF
EQFIDRFPTLEALADADEDEVLKAWEGLGYYSRVRNLHAAVKEVKTRYGG
KVPDDPDEFSRLKGVGPYTVGAVLSLAYGVPEPAVDGNVMRVLSRLFLVT
DDIAKCSTRKRFEQIVREIMAYENPGAFNEALIELGALVCTPRRPSCLLC
PVQAYCQAFAEGVAEELPVKMVKQVPLAVAVLADDEGRVLIRKRDSTGLL
ANLWEFPSCETDGADGKEKLEQMVGLQVELTEPIVSFEHAFSHLVWQLTV
FPGRLVHGGPVEEPYRLAPEDELKAYAFPVSHQRVWREYKEWAS
3D structure
PDB3g0q Atomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylase.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E43 Y126 D144
Catalytic site (residue number reindexed from 1) E35 Y118 D136
Enzyme Commision number 3.2.2.31: adenine glycosylase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000701 purine-specific mismatch base pair DNA N-glycosylase activity
GO:0003677 DNA binding
GO:0003824 catalytic activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0019104 DNA N-glycosylase activity
GO:0032357 oxidized purine DNA binding
GO:0034039 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
GO:0035485 adenine/guanine mispair binding
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006298 mismatch repair
GO:0006950 response to stress

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Molecular Function
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Biological Process
External links
PDB RCSB:3g0q, PDBe:3g0q, PDBj:3g0q
PDBsum3g0q
PubMed19841264
UniProtP83847|MUTY_GEOSE Adenine DNA glycosylase (Gene Name=mutY)

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