Structure of PDB 6vji Chain B Binding Site BS01
Receptor Information
>6vji Chain B (length=253) Species:
13616
(Monodelphis domestica) [
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PSLRKFHQLVAPFVGQLVVTVGGNSKKINPNMLEMLRLQDSQVHGKNLYL
NFGLTEDLGLPESFLLPNSGLWLCFHFGLFGSVRASELSRATWKDPIPRL
VLHFAKGFLAFYNCRIYWCLGPTVKPTSDILSEEFDRRQALEALKQASPV
SYTLLDQRYFAGLGNIIKNEVLYLARIHPLSLGSCLTPLNLESLLDHVVS
FSVGWLQKKLEGKPLHHLIYQKEQCPAGHQVMKDSFGPFQRLTWWCPHCQ
PKA
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
6vji Chain B Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
6vji
Unique Structural Features of Mammalian NEIL2 DNA Glycosylase Prime Its Activity for Diverse DNA Substrates and Environments.
Resolution
2.54 Å
Binding residue
(original residue number in PDB)
C294 H298
Binding residue
(residue number reindexed from 1)
C225 H229
Annotation score
1
Enzymatic activity
Enzyme Commision number
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:0008017
microtubule binding
GO:0008270
zinc ion binding
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: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
Cellular Component
GO:0005634
nucleus
GO:0005654
nucleoplasm
GO:0005737
cytoplasm
GO:0015630
microtubule cytoskeleton
GO:0043231
intracellular membrane-bounded organelle
GO:0072686
mitotic spindle
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6vji
,
PDBe:6vji
,
PDBj:6vji
PDBsum
6vji
PubMed
32846144
UniProt
F7AMK3
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