Structure of PDB 3uxh Chain B Binding Site BS04

Receptor Information
>3uxh Chain B (length=230) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNFEPRA
TDKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQ
FPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGG
TAEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEER
KGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ
Ligand information
Ligand IDFAD
InChIInChI=1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
InChIKeyVWWQXMAJTJZDQX-UYBVJOGSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P@](O)(=O)O[P@@](O)(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)n5cnc6c(N)ncnc56)c2cc1C
OpenEye OEToolkits 1.5.0Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)n5cnc6c5ncnc6N)O)O)O)O)O
OpenEye OEToolkits 1.5.0Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](CO[P@@](=O)(O)O[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)n5cnc6c5ncnc6N)O)O)O)O)O
CACTVS 3.341Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH]([CH](O)[CH]4O)n5cnc6c(N)ncnc56)c2cc1C
ACDLabs 10.04O=C2C3=Nc1cc(c(cc1N(C3=NC(=O)N2)CC(O)C(O)C(O)COP(=O)(O)OP(=O)(O)OCC6OC(n5cnc4c(ncnc45)N)C(O)C6O)C)C
FormulaC27 H33 N9 O15 P2
NameFLAVIN-ADENINE DINUCLEOTIDE
ChEMBLCHEMBL1232653
DrugBankDB03147
ZINCZINC000008215434
PDB chain3uxh Chain B Residue 303 [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]
PDB3uxh Design, synthesis, and biological evaluation of potent quinoline and pyrroloquinoline ammosamide analogues as inhibitors of quinone reductase 2.
Resolution1.53 Å
Binding residue
(original residue number in PDB)		H11 S16 F17 N18 S20 P102 L103 Y104 W105 F106 T147 T148 G149 Y155 E193 E197 R200 K201
Binding residue
(residue number reindexed from 1)		H11 S16 F17 N18 S20 P102 L103 Y104 W105 F106 T147 T148 G149 Y155 E193 E197 R200 K201
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G149 Y155 N161
Catalytic site (residue number reindexed from 1) G149 Y155 N161
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:3uxh, PDBe:3uxh, PDBj:3uxh
PDBsum3uxh
PubMed22206487
UniProtP16083|NQO2_HUMAN Ribosyldihydronicotinamide dehydrogenase [quinone] (Gene Name=NQO2)

[Back to BioLiP]