Structure of PDB 1l1z Chain A Binding Site BS02
Receptor Information
>1l1z Chain A (length=263) Species:
1422
(Geobacillus stearothermophilus) [
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PELPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKFGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDQTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMKGGSTVGTFQHHLYVYGRQGNPCKRCGTPIEKTVV
AGRGTHYCPRCQR
Ligand information
>1l1z Chain C (length=12) [
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gtccacgtctac
Receptor-Ligand Complex Structure
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PDB
1l1z
Structural insights into lesion recognition and repair by the bacterial 8-oxoguanine DNA glycosylase MutM.
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
P2 E3 K60 H74 R76 M77 R112 F114 N174 Y242 K258 R264
Binding residue
(residue number reindexed from 1)
P1 E2 K59 H73 R75 M76 R111 F113 N173 Y231 K247 R253
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:1l1z
,
PDBe:1l1z
,
PDBj:1l1z
PDBsum
1l1z
PubMed
12055620
UniProt
P84131
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