Structure of PDB 3jr4 Chain A Binding Site BS02

Receptor Information
>3jr4 Chain A (length=263) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PQLPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKFGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDQTVVAGFGCIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMKGGSTAGTFQHHLYVYGRQGNPCKRCGTPIEKTVV
AGRGTHYCPRCQR
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3jr4 Entrapment and structure of an extrahelical guanine attempting to enter the active site of a bacterial DNA glycosylase, MutM.
Resolution2.601 Å
Binding residue
(original residue number in PDB)		Q3 K60 H74 R76 M77 E78 R112 C174 I175 Y242 K258 R264 G265
Binding residue
(residue number reindexed from 1)		Q2 K59 H73 R75 M76 E77 R111 C173 I174 Y231 K247 R253 G254
Enzymatic activity
Catalytic site (original residue number in PDB) P2 Q3
Catalytic site (residue number reindexed from 1) P1 Q2
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:0003677 DNA 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:0016787 hydrolase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0016829 lyase activity
GO:0019104 DNA N-glycosylase activity
GO:0034039 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
GO:0046872 metal ion binding
GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease 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:3jr4, PDBe:3jr4, PDBj:3jr4
PDBsum3jr4
PubMed19889642
UniProtP84131

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