Structure of PDB 3gq4 Chain A Binding Site BS02
Receptor Information
>3gq4 Chain A (length=273) Species:
1422
(Geobacillus stearothermophilus) [
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PQLPEVETIRRTLLPLIVGKTIEDVRIFWPNIIRHPRDSEAFAARMIGQT
VRGLERRGKFLKFLLDRDALISHLRMEGRYAVASALEPLEPHTHVVFCFT
DGSELRYRDVRKFGTMHVYAKEEADRRPPLAELGPEPLSPAFSPAVLAER
AVKTKRSVKALLLDCTVVAGFGNIYVDESLFRAGILPGRPAASLSSKEIE
RLHEEMVATIGEAVMKGGSTVRTYVNTQGEAGTFQHHLYVYGRQGNPCKR
CGTPIEKTVVAGRGTHYCPRCQR
Ligand information
>3gq4 Chain C (length=12) [
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cgtccgggtcta
Receptor-Ligand Complex Structure
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PDB
3gq4
Encounter and extrusion of an intrahelical lesion by a DNA repair enzyme.
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
P2 Q3 E6 K60 H74 R76 M77 R112 F114 G173 N174 I175 T221 V222 R223 T224 Y225 Y242 K258 R264
Binding residue
(residue number reindexed from 1)
P1 Q2 E5 K59 H73 R75 M76 R111 F113 G172 N173 I174 T220 V221 R222 T223 Y224 Y241 K257 R263
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:3gq4
,
PDBe:3gq4
,
PDBj:3gq4
PDBsum
3gq4
PubMed
20010681
UniProt
P84131
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