Structure of PDB 1kfv Chain A Binding Site BS02
Receptor Information
>1kfv Chain A (length=264) Species:
1358
(Lactococcus lactis) [
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GELPEVETVRRELEKRIVGQKIISIEATYPRMVLTGFEQLKKELTGKTIQ
GISRRGKYLIFEIGDDFRLISHLRMEGKYRLATLDAPREKHDHLTMKFAD
GQLIYADVRKFGTWELISTDQVLPYFLKKKIGPEPTYEDFDEKLFREKLR
KSTKKIKPYLLEQTLVAGLGNIYVDEVLWLAKIHPEKETNQLIESSIHLL
HDSIIEILQKAIKLGGSSISTGKMQNELQVYGKTGEKCSRCGAEIQKIKV
AGRGTHFCPVCQQK
Ligand information
>1kfv Chain E (length=13) [
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gagaaacaaagag
Receptor-Ligand Complex Structure
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PDB
1kfv
Crystal structure of the Lactococcus lactis formamidopyrimidine-DNA glycosylase bound to an abasic site analogue-containing DNA.
Resolution
2.55 Å
Binding residue
(original residue number in PDB)
H91 V108 R109 F111
Binding residue
(residue number reindexed from 1)
H91 V108 R109 F111
Binding affinity
PDBbind-CN
: Kd=6nM
Enzymatic activity
Catalytic site (original residue number in PDB)
G1
Catalytic site (residue number reindexed from 1)
G1
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
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Biological Process
External links
PDB
RCSB:1kfv
,
PDBe:1kfv
,
PDBj:1kfv
PDBsum
1kfv
PubMed
12065399
UniProt
P42371
|FPG_LACLC Formamidopyrimidine-DNA glycosylase (Gene Name=mutM)
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