Structure of PDB 6rp0 Chain A Binding Site BS02
Receptor Information
>6rp0 Chain A (length=266) Species:
1359
(Lactococcus cremoris) [
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PELPEVETVRRELEKRIVGQKIISIEATYPRMVLTGFEQLKKELTGKTIQ
GISRRGKYLIFEIGDDFRLISHLRMEGKYRLATLDAPREKHDHLTMKFAD
GQLIYADVRKFGTWELISTDQVLPYFLKKKIGPEPTYEDFDEKLFREKLR
KSTKKIKPYLLEQTLVAGLGNIYVDEVLWLAKIHPEKETNQLIESSIHLL
HDSIIEILQKAIKLGGSSALGSTGKMQNELQVYGKTGEKCSRCGAEIQKI
KVAGRGTHFCPVCQQK
Ligand information
>6rp0 Chain C (length=14) [
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gcgagaaacaaaga
Receptor-Ligand Complex Structure
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PDB
6rp0
Thiopurine Derivative-Induced Fpg/Nei DNA Glycosylase Inhibition: Structural, Dynamic and Functional Insights.
Resolution
2.25 Å
Binding residue
(original residue number in PDB)
K90 H91 V108 R109 K110 F111 K154
Binding residue
(residue number reindexed from 1)
K90 H91 V108 R109 K110 F111 K154
Enzymatic activity
Catalytic site (original residue number in PDB)
P1 E2
Catalytic site (residue number reindexed from 1)
P1 E2
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:6rp0
,
PDBe:6rp0
,
PDBj:6rp0
PDBsum
6rp0
PubMed
32192183
UniProt
P42371
|FPG_LACLC Formamidopyrimidine-DNA glycosylase (Gene Name=mutM)
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