Structure of PDB 5lbt Chain B Binding Site BS04

Receptor Information
>5lbt Chain B (length=226) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRAT
DKDITGTPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLY
WFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEM
YTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMV
AAWSQRLQTIWKEEPIPCTAHWHFGQ
Ligand information
Ligand ID6T0
InChIInChI=1S/C14H16N4/c1-9(2)7-18-8-16-12-13(18)10-5-3-4-6-11(10)17-14(12)15/h3-6,8-9H,7H2,1-2H3,(H2,15,17)
InChIKeyDOUYETYNHWVLEO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.5CC(C)Cn1cnc2c1c3ccccc3nc2N
CACTVS 3.385CC(C)Cn1cnc2c(N)nc3ccccc3c12
FormulaC14 H16 N4
Name1-(2-methylpropyl)imidazo[4,5-c]quinolin-4-amine
ChEMBLCHEMBL1282
DrugBankDB00724
ZINCZINC000019632912
PDB chain5lbt Chain B Residue 304 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5lbt Imiquimod Inhibits Mitochondrial Complex I and Induces K+ efflux-independent Nlrp3 Inflammasome Activation via Nek7
Resolution1.75 Å
Binding residue
(original residue number in PDB)		N23 D27
Binding residue
(residue number reindexed from 1)		N22 D26
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G149 Y155 N161
Catalytic site (residue number reindexed from 1) G145 Y151 N157
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

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Cellular Component
External links
PDB RCSB:5lbt, PDBe:5lbt, PDBj:5lbt
PDBsum5lbt
PubMed
UniProtP16083|NQO2_HUMAN Ribosyldihydronicotinamide dehydrogenase [quinone] (Gene Name=NQO2)

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