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 T84581 Target Info
Target Name Cytoplasmic thioredoxin reductase (TXNRD1)
Synonyms Thioredoxin reductase TR1; Thioredoxin reductase 1, cytoplasmic; KM-102-derived reductase-like factor; KDRF; Gene associated with retinoic and interferon-induced mortality 12 protein; Gene associated with retinoic and IFN-induced mortality 12 protein; GRIM12; GRIM-12
Target Type Successful Target
Gene Name TXNRD1
Biochemical Class Sulfur donor oxidoreductase
UniProt ID
TRXR1_HUMAN
Ligand General Information  Top
Ligand Name Flavin-Adenine Dinucleotide Ligand Info
Canonical SMILES CC1=CC2=C(C=C1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=NC6=C(N=CN=C65)N)O)O)O)O)O
InChI 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
InChIKey VWWQXMAJTJZDQX-UYBVJOGSSA-N
PubChem Compound ID 643975
Drug Binding Sites of Target  Top
PDB ID: 2CFY      Crystal structure of human thioredoxin reductase 1
Method X-ray diffraction Resolution 2.70 Å Mutation No [1]
PDB Sequence
SYDYDLIIIG
19
GGSGGLAAAK
29
EAAQYGKKVM
39
VLDFVTPTPL
49
GTRWGLGGTC
59

VNVGCIPKKL
69
MHQAALLGQA
79
LQDSRNYGWK
89
VEETVKHDWD
99
RMIEAVQNHI
109

GSLNWGYRVA
119
LREKKVVYEN
129
AYGQFIGPHR
139
IKATNNKGKE
149
KIYSAERFLI
159

ATGERPRYLG
169
IPGDKEYCIS
179
SDDLFSLPYC
189
PGKTLVVGAS
199
YVALECAGFL
209

AGIGLDVTVM
219
VRSILLRGFD
229
QDMANKIGEH
239
MEEHGIKFIR
249
QFVPIKVEQI
259

EAGTPGRLRV
269
VAQSTNSEEI
279
IEGEYNTVML
289
AIGRDACTRK
299
IGLETVGVKI
309

NEKTGKIPVT
319
DEEQTNVPYI
329
YAIGDILEDK
339
VELTPVAIQA
349
GRLLAQRLYA
359

GSTVKCDYEN
369
VPTTVFTPLE
379
YGACGLSEEK
389
AVEKFGEENI
399
EVYHSYFWPL
409

EWTIPSRDNN
419
KCYAKIICNT
429
KDNERVVGFH
439
VLGPNAGEVT
449
QGFAAALKCG
459

LTKKQLDSTI
469
GIHPVCAEVF
479
TTLSVTKRSG
489
ASIL
Residue
Distance (Å)
ILE18
3.588
GLY19
3.108
GLY20
3.602
GLY21
3.194
SER22
3.468
GLY23
3.219
GLY24
4.179
LEU41
3.401
ASP42
3.035
PHE43
2.822
VAL44
3.686
THR45
4.851
TRP53
4.796
GLY56
4.492
GLY57
3.459
THR58
2.578
CYS59
3.366
VAL62
3.850
GLY63
3.605
CYS64
2.904
LYS67
2.425
ALA130
3.579
TYR131
3.204
Residue
Distance (Å)
GLY132
2.908
ALA160
3.537
THR161
2.723
GLY162
3.449
GLU163
4.691
SER180
3.956
PHE184
4.273
TYR200
3.450
VAL201
3.148
GLU204
4.078
ARG293
3.252
CYS296
4.463
ILE300
3.365
ILE332
4.293
GLY333
3.254
ASP334
2.975
GLU341
3.495
LEU342
3.559
THR343
3.326
PRO344
3.241
ALA346
4.070
THR373
4.616
PHE375
3.783
PDB ID: 3QFA      Crystal structure of the human thioredoxin reductase-thioredoxin complex
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [2]
PDB Sequence
DLPKSYDYDL
15
IIIGGGSGGL
25
AAAKEAAQYG
35
KKVMVLDFVT
45
PTPLGTRWGL
55

GGTCVNVGCI
65
PKKLMHQAAL
75
LGQALQDSRN
85
YGWKVEETVK
95
HDWDRMIEAV
105

QNHIGSLNWG
115
YRVALREKKV
125
VYENAYGQFI
135
GPHRIKATNN
145
KGKEKIYSAE
155

RFLIATGERP
165
RYLGIPGDKE
175
YCISSDDLFS
185
LPYCPGKTLV
195
VGASYVALEC
205

AGFLAGIGLD
215
VTVMVRSILL
225
RGFDQDMANK
235
IGEHMEEHGI
245
KFIRQFVPIK
255

VEQIEAGTPG
265
RLRVVAQSTN
275
SEEIIEGEYN
285
TVMLAIGRDA
295
CTRKIGLETV
305

GVKINEKTGK
315
IPVTDEEQTN
325
VPYIYAIGDI
335
LEDKVELTPV
345
AIQAGRLLAQ
355

RLYAGSTVKC
365
DYENVPTTVF
375
TPLEYGACGL
385
SEEKAVEKFG
395
EENIEVYHSY
405

FWPLEWTIPS
415
RDNNKCYAKI
425
ICNTKDNERV
435
VGFHVLGPNA
445
GEVTQGFAAA
455

LKCGLTKKQL
465
DSTIGIHPVC
475
AEVFTTLSVT
485
KRSGASILQA
495
GSCG
Residue
Distance (Å)
ILE18
3.490
GLY19
3.043
GLY20
3.725
GLY21
3.281
SER22
3.253
GLY23
2.858
GLY24
4.143
LEU41
3.392
ASP42
2.579
PHE43
2.662
VAL44
3.854
THR45
4.945
GLY56
4.616
GLY57
3.726
THR58
2.824
CYS59
3.185
VAL62
3.537
GLY63
3.452
CYS64
3.314
LYS67
2.723
ALA130
3.665
TYR131
3.048
GLY132
2.804
Residue
Distance (Å)
ALA160
3.356
THR161
3.105
GLY162
3.436
GLU163
4.187
SER180
3.548
PHE184
3.778
TYR200
3.328
VAL201
3.635
GLU204
4.579
ARG293
3.229
CYS296
4.391
ILE300
3.395
ILE332
4.151
GLY333
2.983
ASP334
2.766
ILE335
4.782
GLU341
3.200
LEU342
3.424
THR343
3.199
PRO344
3.330
ALA346
3.754
THR373
4.967
PHE375
3.994
PDB ID: 3QFB      Crystal structure of the human thioredoxin reductase-thioredoxin complex
Method X-ray diffraction Resolution 2.60 Å Mutation Yes [2]
PDB Sequence
EDLPKSYDYD
14
LIIIGGGSGG
24
LAAAKEAAQY
34
GKKVMVLDFV
44
TPTPLGTRWG
54

LGGTCVNVGC
64
IPKKLMHQAA
74
LLGQALQDSR
84
NYGWKVEETV
94
KHDWDRMIEA
104

VQNHIGSLNW
114
GYRVALREKK
124
VVYENAYGQF
134
IGPHRIKATN
144
NKGKEKIYSA
154

ERFLIATGER
164
PRYLGIPGDK
174
EYCISSDDLF
184
SLPYCPGKTL
194
VVGASYVALE
204

CAGFLAGIGL
214
DVTVMVRSIL
224
LRGFDQDMAN
234
KIGEHMEEHG
244
IKFIRQFVPI
254

KVEQIEAGTP
264
GRLRVVAQST
274
NSEEIIEGEY
284
NTVMLAIGRD
294
ACTRKIGLET
304

VGVKINEKTG
314
KIPVTDEEQT
324
NVPYIYAIGD
334
ILEDKVELTP
344
VAIQAGRLLA
354

QRLYAGSTVK
364
CDYENVPTTV
374
FTPLEYGACG
384
LSEEKAVEKF
394
GEENIEVYHS
404

YFWPLEWTIP
414
SRDNNKCYAK
424
IICNTKDNER
434
VVGFHVLGPN
444
AGEVTQGFAA
454

ALKCGLTKKQ
464
LDSTIGIHPV
474
CAEVFTTLSV
484
TKRSGASILQ
494
AGSCG
Residue
Distance (Å)
ILE18
3.739
GLY19
3.156
GLY20
3.433
GLY21
3.098
SER22
3.127
GLY23
2.658
GLY24
4.054
LEU41
3.269
ASP42
3.060
PHE43
3.233
VAL44
3.802
THR45
4.999
TRP53
4.770
GLY56
4.792
GLY57
3.445
THR58
2.588
CYS59
3.060
VAL62
3.689
GLY63
3.627
CYS64
3.468
LYS67
2.621
ALA130
3.722
TYR131
3.183
GLY132
3.162
Residue
Distance (Å)
ALA160
3.231
THR161
3.335
GLY162
3.471
GLU163
4.060
ARG164
4.647
SER180
3.999
PHE184
4.072
TYR200
3.605
VAL201
3.788
GLU204
4.600
ARG293
3.243
CYS296
4.171
ILE300
3.523
ILE332
4.216
GLY333
3.017
ASP334
2.815
GLU341
3.567
LEU342
3.356
THR343
3.127
PRO344
3.141
ALA346
3.935
THR373
4.988
PHE375
4.064
PDB ID: 2J3N      X-ray structure of human thioredoxin reductase 1
Method X-ray diffraction Resolution 2.80 Å Mutation No [3]
PDB Sequence
SYDYDLIIIG
19
GGSGGLAAAK
29
EAAQYGKKVM
39
VLDFVTPTPL
49
GTRWGLGGTC
59

VNVGCIPKKL
69
MHQAALLGQA
79
LQDSRNYGWK
89
VEETVKHDWD
99
RMIEAVQNHI
109

GSLNWGYRVA
119
LREKKVVYEN
129
AYGQFIGPHR
139
IKATNNKGKE
149
KIYSAERFLI
159

ATGERPRYLG
169
IPGDKEYCIS
179
SDDLFSLPYC
189
PGKTLVVGAS
199
YVALECAGFL
209

AGIGLDVTVM
219
VRSILLRGFD
229
QDMANKIGEH
239
MEEHGIKFIR
249
QFVPIKVEQI
259

EAGTPGRLRV
269
VAQSTNSEEI
279
IEGEYNTVML
289
AIGRDACTRK
299
IGLETVGVKI
309

NEKTGKIPVT
319
DEEQTNVPYI
329
YAIGDILEDK
339
VELTPVAIQA
349
GRLLAQRLYA
359

GSTVKCDYEN
369
VPTTVFTPLE
379
YGACGLSEEK
389
AVEKFGEENI
399
EVYHSYFWPL
409

EWTIPSRDNN
419
KCYAKIICNT
429
KDNERVVGFH
439
VLGPNAGEVT
449
QGFAAALKCG
459

LTKKQLDSTI
469
GIHPVCAEVF
479
TTLSVTKRSG
489
ASILQAG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:18 or .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:41 or .A:42 or .A:43 or .A:44 or .A:45 or .A:53 or .A:56 or .A:57 or .A:58 or .A:59 or .A:62 or .A:63 or .A:64 or .A:67 or .A:130 or .A:131 or .A:132 or .A:160 or .A:161 or .A:162 or .A:163 or .A:164 or .A:180 or .A:184 or .A:200 or .A:201 or .A:204 or .A:293 or .A:296 or .A:299 or .A:300 or .A:332 or .A:333 or .A:334 or .A:335 or .A:341 or .A:342 or .A:343 or .A:344 or .A:346 or .A:375; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE18
3.569
GLY19
3.057
GLY20
3.626
GLY21
3.293
SER22
3.553
GLY23
2.770
GLY24
4.012
LEU41
3.409
ASP42
2.904
PHE43
3.180
VAL44
3.874
THR45
4.867
TRP53
4.873
GLY56
4.631
GLY57
3.086
THR58
2.805
CYS59
3.230
VAL62
4.169
GLY63
3.939
CYS64
3.334
LYS67
2.655
ALA130
3.907
TYR131
3.162
GLY132
3.044
Residue
Distance (Å)
ALA160
3.494
THR161
3.397
GLY162
3.192
GLU163
3.923
ARG164
4.166
SER180
3.761
PHE184
4.380
TYR200
3.655
VAL201
3.196
GLU204
4.480
ARG293
3.391
CYS296
4.128
LYS299
4.955
ILE300
3.719
ILE332
4.492
GLY333
4.003
ASP334
2.690
ILE335
4.806
GLU341
3.481
LEU342
3.593
THR343
2.942
PRO344
2.910
ALA346
3.733
PHE375
4.246
PDB ID: 2ZZC      Crystal structure of NADP(H):human thioredoxin reductase I
Method X-ray diffraction Resolution 2.60 Å Mutation No [4]
PDB Sequence
SYDYDLIIIG
19
GGSGGLAAAK
29
EAAQYGKKVM
39
VLDFVTPTPL
49
GTRWGLGGTC
59

VNVGCIPKKL
69
MHQAALLGQA
79
LQDSRNYGWK
89
VEETVKHDWD
99
RMIEAVQNHI
109

GSLNWGYRVA
119
LREKKVVYEN
129
AYGQFIGPHR
139
IKATNNKGKE
149
KIYSAERFLI
159

ATGERPRYLG
169
IPGDKEYCIS
179
SDDLFSLPYC
189
PGKTLVVGAS
199
YVALECAGFL
209

AGIGLDVTVM
219
VRSILLRGFD
229
QDMANKIGEH
239
MEEHGIKFIR
249
QFVPIKVEQI
259

EAGTPGRLRV
269
VAQSTNSEEI
279
IEGEYNTVML
289
AIGRDACTRK
299
IGLETVGVKI
309

NEKTGKIPVT
319
DEEQTNVPYI
329
YAIGDILEDK
339
VELTPVAIQA
349
GRLLAQRLYA
359

GSTVKCDYEN
369
VPTTVFTPLE
379
YGACGLSEEK
389
AVEKFGEENI
399
EVYHSYFWPL
409

EWTIPSRDNN
419
KCYAKIICNT
429
KDNERVVGFH
439
VLGPNAGEVT
449
QGFAAALKCG
459

LTKKQLDSTI
469
GIHPVCAEVF
479
TTLSVTKRSG
489
ASILQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:18 or .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:41 or .A:42 or .A:43 or .A:44 or .A:53 or .A:56 or .A:57 or .A:58 or .A:59 or .A:62 or .A:63 or .A:64 or .A:67 or .A:130 or .A:131 or .A:132 or .A:160 or .A:161 or .A:162 or .A:163 or .A:164 or .A:180 or .A:184 or .A:201 or .A:204 or .A:293 or .A:296 or .A:300 or .A:332 or .A:333 or .A:334 or .A:341 or .A:342 or .A:343 or .A:344 or .A:346 or .A:375; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE18
3.531
GLY19
3.332
GLY20
4.056
GLY21
3.268
SER22
3.283
GLY23
2.858
GLY24
4.006
LEU41
3.565
ASP42
3.210
PHE43
2.802
VAL44
3.967
TRP53
4.990
GLY56
4.769
GLY57
3.520
THR58
2.521
CYS59
3.539
VAL62
3.415
GLY63
3.421
CYS64
3.300
LYS67
3.208
ALA130
3.486
TYR131
3.269
Residue
Distance (Å)
GLY132
2.867
ALA160
3.568
THR161
3.251
GLY162
3.154
GLU163
4.477
ARG164
4.588
SER180
3.825
PHE184
3.931
VAL201
4.070
GLU204
4.853
ARG293
3.326
CYS296
4.570
ILE300
4.000
ILE332
4.273
GLY333
2.962
ASP334
2.821
GLU341
3.047
LEU342
3.127
THR343
3.109
PRO344
3.054
ALA346
4.091
PHE375
4.105
PDB ID: 2ZZ0      Crystal structure of human thioredoxin reductase I (SeCys 498 Cys)
Method X-ray diffraction Resolution 2.80 Å Mutation No [4]
PDB Sequence
KSYDYDLIII
18
GGGSGGLAAA
28
KEAAQYGKKV
38
MVLDFVTPTP
48
LGTRWGLGGT
58

CVNVGCIPKK
68
LMHQAALLGQ
78
ALQDSRNYGW
88
KVEETVKHDW
98
DRMIEAVQNH
108

IGSLNWGYRV
118
ALREKKVVYE
128
NAYGQFIGPH
138
RIKATNNKGK
148
EKIYSAERFL
158

IATGERPRYL
168
GIPGDKEYCI
178
SSDDLFSLPY
188
CPGKTLVVGA
198
SYVALECAGF
208

LAGIGLDVTV
218
MVRSILLRGF
228
DQDMANKIGE
238
HMEEHGIKFI
248
RQFVPIKVEQ
258

IEAGTPGRLR
268
VVAQSTNSEE
278
IIEGEYNTVM
288
LAIGRDACTR
298
KIGLETVGVK
308

INEKTGKIPV
318
TDEEQTNVPY
328
IYAIGDILED
338
KVELTPVAIQ
348
AGRLLAQRLY
358

AGSTVKCDYE
368
NVPTTVFTPL
378
EYGACGLSEE
388
KAVEKFGEEN
398
IEVYHSYFWP
408

LEWTIPSRDN
418
NKCYAKIICN
428
TKDNERVVGF
438
HVLGPNAGEV
448
TQGFAAALKC
458

GLTKKQLDST
468
IGIHPVCAEV
478
FTTLSVTKRS
488
GASILQAGCC
498
G
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:18 or .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:41 or .A:42 or .A:43 or .A:44 or .A:45 or .A:56 or .A:57 or .A:58 or .A:59 or .A:62 or .A:63 or .A:64 or .A:67 or .A:130 or .A:131 or .A:132 or .A:160 or .A:161 or .A:162 or .A:163 or .A:164 or .A:180 or .A:184 or .A:200 or .A:201 or .A:204 or .A:293 or .A:296 or .A:300 or .A:332 or .A:333 or .A:334 or .A:335 or .A:341 or .A:342 or .A:343 or .A:344 or .A:346 or .A:373 or .A:375; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE18
3.662
GLY19
3.357
GLY20
4.027
GLY21
3.253
SER22
3.283
GLY23
3.129
GLY24
3.953
LEU41
3.453
ASP42
2.951
PHE43
2.745
VAL44
3.598
THR45
4.918
GLY56
4.806
GLY57
3.491
THR58
3.045
CYS59
3.435
VAL62
3.528
GLY63
3.531
CYS64
3.456
LYS67
2.762
ALA130
3.456
TYR131
3.456
GLY132
3.003
ALA160
3.868
Residue
Distance (Å)
THR161
3.058
GLY162
3.239
GLU163
4.603
ARG164
4.389
SER180
3.889
PHE184
4.071
TYR200
3.341
VAL201
3.753
GLU204
4.551
ARG293
3.108
CYS296
4.643
ILE300
3.485
ILE332
4.222
GLY333
2.834
ASP334
2.803
ILE335
4.928
GLU341
3.008
LEU342
2.956
THR343
3.033
PRO344
3.583
ALA346
3.980
THR373
4.876
PHE375
3.910
PDB ID: 2ZZB      Crystal structure of human thioredoxin reductase I and terpyridine platinum(II)
Method X-ray diffraction Resolution 3.20 Å Mutation No [4]
PDB Sequence
SYDYDLIIIG
19
GGSGGLAAAK
29
EAAQYGKKVM
39
VLDFVTPTPL
49
GTRWGLGGTC
59

VNVGCIPKKL
69
MHQAALLGQA
79
LQDSRNYGWK
89
VEETVKHDWD
99
RMIEAVQNHI
109

GSLNWGYRVA
119
LREKKVVYEN
129
AYGQFIGPHR
139
IKATNNKGKE
149
KIYSAERFLI
159

ATGERPRYLG
169
IPGDKEYCIS
179
SDDLFSLPYC
189
PGKTLVVGAS
199
YVALECAGFL
209

AGIGLDVTVM
219
VRSILLRGFD
229
QDMANKIGEH
239
MEEHGIKFIR
249
QFVPIKVEQI
259

EAGTPGRLRV
269
VAQSTNSEEI
279
IEGEYNTVML
289
AIGRDACTRK
299
IGLETVGVKI
309

NEKTGKIPVT
319
DEEQTNVPYI
329
YAIGDILEDK
339
VELTPVAIQA
349
GRLLAQRLYA
359

GSTVKCDYEN
369
VPTTVFTPLE
379
YGACGLSEEK
389
AVEKFGEENI
399
EVYHSYFWPL
409

EWTIPSRDNN
419
KCYAKIICNT
429
KDNERVVGFH
439
VLGPNAGEVT
449
QGFAAALKCG
459

LTKKQLDSTI
469
GIHPVCAEVF
479
TTLSVTKRSG
489
ASILQAGCCG
499
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
ILE18
3.476
GLY19
3.173
GLY20
3.773
GLY21
2.840
SER22
3.097
GLY23
3.388
GLY24
3.967
LEU41
3.468
ASP42
3.186
PHE43
2.754
VAL44
3.494
THR45
4.768
TRP53
4.726
GLY56
4.849
GLY57
3.561
THR58
2.457
CYS59
3.195
VAL62
3.310
GLY63
3.421
CYS64
3.199
LYS67
2.710
ALA130
3.366
TYR131
3.391
Residue
Distance (Å)
GLY132
2.971
ALA160
3.510
THR161
3.159
GLY162
3.624
GLU163
4.808
ARG164
4.763
SER180
3.884
PHE184
4.069
TYR200
2.875
VAL201
3.506
GLU204
4.615
ARG293
3.532
CYS296
4.550
ILE300
3.543
ILE332
4.054
GLY333
3.182
ASP334
2.554
GLU341
3.407
LEU342
3.267
THR343
3.312
PRO344
3.463
ALA346
4.152
PHE375
4.525
References  Top
REF 1 Crystal Structure of Human Thioredoxin Reductase 1
REF 2 Crystal structure of the human thioredoxin reductase-thioredoxin complex. Nat Commun. 2011 Jul 12;2:383.
REF 3 The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis. J Mol Biol. 2007 Jun 29;370(1):116-27.
REF 4 Terpyridine-platinum(II) complexes are effective inhibitors of mammalian topoisomerases and human thioredoxin reductase 1. J Inorg Biochem. 2009 Jul;103(7):1082-92.

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