Structure of PDB 4qod Chain B

Receptor sequence
>4qodB (length=229) Species: 9606 (Homo sapiens) [Search protein sequence]
GKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNFEPRAT
DKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQF
PLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGT
AEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERK
GMVAAWSQRLQTIWKEEPIPCTAHWHFGQ
3D structure
PDB4qod The value crystal structure of apo quinone reductase 2 at 1.35A
ChainB
Resolution1.35 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN B H173 H177 C222 H172 H176 C221
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:4qod, PDBe:4qod, PDBj:4qod
PDBsum4qod
PubMed
UniProtP16083|NQO2_HUMAN Ribosyldihydronicotinamide dehydrogenase [quinone] (Gene Name=NQO2)

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