Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T52389 Target Info
Target Name Quinone reductase 1 (NQO1)
Synonyms Qui reductase 1; QR1; Phylloquinone reductase; Phylloqui reductase; NMOR1; NAD(P)H:quinone oxidoreductase 1; NAD(P)H dehydrogenase [quinone] 1; Menadione reductase; DTD; DT-diaphorase 1; DT-diaphorase; DIA4; Azoreductase
Target Type Clinical trial Target
Gene Name NQO1
Biochemical Class NADH/NADPH oxidoreductase
UniProt ID
NQO1_HUMAN
Ligand General Information  Top
Ligand Name Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone] Ligand Info
Canonical SMILES C1=CC=C2C(=C1)C(=O)C(C(=O)O2)CC3C(=O)C4=CC=CC=C4OC3=O
InChI 1S/C19H12O6/c20-16-10-5-1-3-7-14(10)24-18(22)12(16)9-13-17(21)11-6-2-4-8-15(11)25-19(13)23/h1-8,12-13H,9H2/t12-,13+
InChIKey HIZKPJUTKKJDGA-BETUJISGSA-N
PubChem Compound ID 17753965
Drug Binding Sites of Target  Top
PDB ID: 5FUQ      CRYSTAL STRUCTURE OF THE H80R VARIANT OF NQO1 BOUND TO DICOUMAROL
Method X-ray diffraction Resolution 2.04 Å Mutation Yes [1]
PDB Sequence
MVGRRALIVL
10
AHSERTSFNY
20
AMKEAAAAAL
30
KKKGWEVVES
40
DLYAMNFNPI
50

ISRKDITGKL
60
KDPANFQYPA
70
ESVLAYKEGR
80
LSPDIVAEQK
90
KLEAADLVIF
100

QFPLQWFGVP
110
AILKGWFERV
120
FIGEFAYTYA
130
AMYDKGPFRS
140
KKAVLSITTG
150

GSGSMYSLQG
160
IHGDMNVILW
170
PIQSGILHFC
180
GFQVLEPQLT
190
YSIGHTPADA
200

RIQILEGWKK
210
RLENIWDETP
220
LYFAPSSLFD
230
LNFQAGFLMK
240
KEVQDEEKNK
250

KFGLSVGHHL
260
GKSIPTDNQI
270
KAR
Residue
Distance (Å)
TRP106
3.775
PHE107
3.850
GLY150
3.365
GLY151
3.429
SER152
4.540
Residue
Distance (Å)
MET155
3.629
TYR156
4.554
HIS162
2.825
SER192
3.885
HIS195
3.032
PDB ID: 2F1O      Crystal Structure of NQO1 with Dicoumarol
Method X-ray diffraction Resolution 2.75 Å Mutation No [2]
PDB Sequence
VGRRALIVLA
10
HSERTSFNYA
20
MKEAAAAALK
30
KKGWEVVESD
40
LYAMNFNPII
50

SRKDITGKLK
60
DPANFQYPAE
70
SVLAYKEGHL
80
SPDIVAEQKK
90
LEAADLVIFQ
100

FPLQWFGVPA
110
ILKGWFERVF
120
IGEFAYTYAA
130
MYDKGPFRSK
140
KAVLSITTGG
150

SGSMYSLQGI
160
HGDMNVILWP
170
IQSGILHFCG
180
FQVLEPQLTY
190
SIGHTPADAR
200

IQILEGWKKR
210
LENIWDETPL
220
YFAPSSLFDL
230
NFQAGFLMKK
240
EVQDEEKNKK
250

FGLSVGHHLG
260
KSIPTDNQIK
270
ARK
Residue
Distance (Å)
TYR126
3.563
TYR128
2.635
MET131
3.833
Residue
Distance (Å)
GLY174
4.623
PHE178
3.364
PHE236
3.222
PDB ID: 4CET      Crystal structure of the complex of the P187S variant of human NAD(P) H:quinone oxidoreductase with dicoumarol at 2.2 A resolution
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [3]
PDB Sequence
GRRALIVLAH
12
SERTSFNYAM
22
KEAAAAALKK
32
KGWEVVESDL
42
YAMNFNPIIS
52

RKDITGKLKD
62
PANFQYPAES
72
VLAYKEGHLS
82
PDIVAEQKKL
92
EAADLVIFQF
102

PLQWFGVPAI
112
LKGWFERVFI
122
GEFAYTYAAM
132
YDKGPFRSKK
142
AVLSITTGGS
152

GSMYSLQGIH
162
GDMNVILWPI
172
QSGILHFCGF
182
QVLESQLTYS
192
IGHTPADARI
202

QILEGWKKRL
212
ENIWDETPLY
222
FA
Residue
Distance (Å)
TRP106
3.483
PHE107
4.571
GLY150
3.467
GLY151
3.408
Residue
Distance (Å)
MET155
3.599
TYR156
3.388
ILE161
3.602
HIS162
2.689
References  Top
REF 1 Identification of Novel Structural Hot-Spots for the Correction of Functional and Stability Defects in a Cancer-Associated Polymorphic Nadph:Quinone Oxidoreductase 1 from Sequence-Alignment Statistics.
REF 2 The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry. 2006 May 23;45(20):6372-8.
REF 3 Collapse of the native structure caused by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase(1.). FEBS J. 2014 Oct;281(20):4691-4704.

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