Structure of PDB 4g4r Chain A Binding Site BS02

Receptor Information
>4g4r Chain A (length=252) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PQLPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKAGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDCTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMHLYVYGRQGNPCKRCGTPIEKTVVAGRGTHYCPRC
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Ligand information
Receptor-Ligand Complex Structure
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PDB4g4r Structural and Biochemical Analysis of DNA Helix Invasion by the Bacterial 8-Oxoguanine DNA Glycosylase MutM.
Resolution1.95 Å
Binding residue
(original residue number in PDB)
Q3 K60 H74 R76 M77 P130 E133 L134 C166 T167 G173 N174 Y242 K258 R264 G265
Binding residue
(residue number reindexed from 1)
Q2 K59 H73 R75 M76 P129 E132 L133 C165 T166 G172 N173 Y220 K236 R242 G243
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:4g4r, PDBe:4g4r, PDBj:4g4r
PDBsum4g4r
PubMed23404556
UniProtP84131

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