Structure of PDB 1r2z Chain A Binding Site BS02

Receptor Information
>1r2z Chain A (length=273) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PQLPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKFGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDQTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMKGGSTVRTYVNTQGEAGTFQHHLYVYGRQGNPCKR
CGTPIEKTVVAGRGTHYCPRCQR
Ligand information
Receptor-Ligand Complex Structure
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PDB1r2z DNA Lesion Recognition by the Bacterial Repair Enzyme MutM.
Resolution1.63 Å
Binding residue
(original residue number in PDB)
Q3 E6 K60 H74 R76 M77 R112 F114 G173 N174 I175 S220 T221 V222 R223 Y225 Y242 K258 R264
Binding residue
(residue number reindexed from 1)
Q2 E5 K59 H73 R75 M76 R111 F113 G172 N173 I174 S219 T220 V221 R222 Y224 Y241 K257 R263
Enzymatic activity
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:1r2z, PDBe:1r2z, PDBj:1r2z
PDBsum1r2z
PubMed14525999
UniProtP84131

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