Structure of PDB 5lbu Chain B Binding Site BS05

Receptor Information
>5lbu Chain B (length=228) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRAT
DKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQF
PLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGT
AEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERK
GMVAAWSQRLQTIWKEEPIPCTAHWHFG
Ligand information
Ligand IDC09
InChIInChI=1S/C13H14N4O/c1-2-18-7-10-16-11-8-5-3-4-6-9(8)15-13(14)12(11)17-10/h3-6H,2,7H2,1H3,(H2,14,15)(H,16,17)
InChIKeyDEVCLHVFELRPIU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6CCOCc1[nH]c2c3ccccc3nc(c2n1)N
CACTVS 3.370CCOCc1[nH]c2c3ccccc3nc(N)c2n1
ACDLabs 12.01n3c1ccccc1c2c(nc(n2)COCC)c3N
FormulaC13 H14 N4 O
Name2-(ethoxymethyl)-1H-imidazo[4,5-c]quinolin-4-amine;
CL097
ChEMBLCHEMBL4081845
DrugBank
ZINCZINC000035855615
PDB chain5lbu Chain B Residue 307 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5lbu Imiquimod Inhibits Mitochondrial Complex I and Induces K+ efflux-independent Nlrp3 Inflammasome Activation via Nek7
Resolution1.65 Å
Binding residue
(original residue number in PDB)		N23 V26 D27
Binding residue
(residue number reindexed from 1)		N22 V25 D26
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G149 Y155 N161
Catalytic site (residue number reindexed from 1) G148 Y154 N160
Enzyme Commision number 1.10.5.1: ribosyldihydronicotinamide dehydrogenase (quinone).
Gene Ontology
Molecular Function
GO:0001512 dihydronicotinamide riboside quinone reductase activity
GO:0003955 NAD(P)H dehydrogenase (quinone) activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0016661 oxidoreductase activity, acting on other nitrogenous compounds as donors
GO:0031404 chloride ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0071949 FAD binding
GO:1904408 melatonin binding
GO:1905594 resveratrol binding
Biological Process
GO:1901662 quinone catabolic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5lbu, PDBe:5lbu, PDBj:5lbu
PDBsum5lbu
PubMed
UniProtP16083|NQO2_HUMAN Ribosyldihydronicotinamide dehydrogenase [quinone] (Gene Name=NQO2)

[Back to BioLiP]