Structure of PDB 3u6e Chain A Binding Site BS02

Receptor Information
>3u6e 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
DGSELRYRDVRKFGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDCTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMHLYVYGRQGNPCKRCGTPIEKTVVAGRGTHYCPRC
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Ligand information
Receptor-Ligand Complex Structure
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PDB3u6e Sequence-dependent structural variation in DNA undergoing intrahelical inspection by the DNA glycosylase MutM.
Resolution1.7 Å
Binding residue
(original residue number in PDB)
K60 H74 R76 R112 F114 P130 L134 C166 T167 N174 R264 G265
Binding residue
(residue number reindexed from 1)
K59 H73 R75 R111 F113 P129 L133 C165 T166 N173 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:3u6e, PDBe:3u6e, PDBj:3u6e
PDBsum3u6e
PubMed22465958
UniProtP84131

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