Structure of PDB 1vrl Chain A

Receptor sequence
>1vrlA (length=346) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
PAREFQRDLLDWFARERRDLPWRKDRDPYKVWVSEVMLQQTRVETVIPYF
EQFIDRFPTLEALADADEDEVLKAWEGLGYYSRVRNLHAAVKEVKTRYGG
KVPDDPDEFSRLKGVGPYTVGAVLSLAYGVPEPAVNGNVMRVLSRLFLVT
DDIAKPSTRKRFEQIVREIMAYENPGAFNEALIELGALVCTPRRPSCLLC
PVQAYCQAFAEGVAEELPVKMKKTAVKQVPLAVAVLADDEGRVLIRKRDS
TGLLANLWEFPSCETDDGKEKLEQMVGLQVELTEPIVSFEHAFSHLVWQL
TVFPGRLVHGGPVEEPYRLAPEDELKAYAFPVSHQRVWREYKEWAS
3D structure
PDB1vrl Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y126 N144
Catalytic site (residue number reindexed from 1) Y118 N136
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:1vrl, PDBe:1vrl, PDBj:1vrl
PDBsum1vrl
PubMed14961129
UniProtP83847|MUTY_GEOSE Adenine DNA glycosylase (Gene Name=mutY)

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