Target Binding Site Detail

Content Navigation (  All   None )                                      
Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T79591 Target Info
Target Name Thyroid hormone receptor alpha (THRA)
Synonyms V-erbA-related protein 7; THRA2; THRA1; Nuclear receptor subfamily 1 group A member 1; NR1A1; ERBA1; EAR7; EAR-7; C-erbA-alpha; C-erbA-1
Target Type Successful Target
Gene Name THRA
Biochemical Class Nuclear hormone receptor
UniProt ID
THA_HUMAN
Ligand General Information  Top
Ligand Name S-(Dimethylarsenic)Cysteine Ligand Info
Canonical SMILES C[As](C)SCC(C(=O)O)N
InChI 1S/C5H12AsNO2S/c1-6(2)10-3-4(7)5(8)9/h4H,3,7H2,1-2H3,(H,8,9)/t4-/m0/s1
InChIKey UKLXSOVDMSQHMM-BYPYZUCNSA-N
PubChem Compound ID 17753880
Drug Binding Sites of Target  Top
PDB ID: 2H79      Crystal Structure of human TR alpha bound T3 in orthorhombic space group
Method X-ray diffraction Resolution 1.87 Å Mutation Yes [1]
PDB Sequence
ARGSHMEEMI
151
RSLQQRPEPT
161
PEEWDLIHIA
171
TEAHRSTNAQ
181
GSHWKQRRKF
191

LPDDIGQSPI
201
VSMPDGDKVD
211
LEAFSEFTKI
221
ITPAITRVVD
231
FAKKLPMFSE
241

LPEDQIILLK
252
GCCMEIMSLR
262
AAVRYDPESD
272
TLTLSGEMAV
282
KREQLKNGGL
292

GVVSDAIFEL
302
GKSLSAFNLD
312
DTEVALLQAV
322
LLMSTDRSGL
332
LVDKIEKSQE
343

AYLLAFEHYV
353
NHRKHNIPHF
363
WPKLLMKVTD
373
LRMIGAHASR
384
FLHKVEPTEL
396

FPPLFLEVFE
406
DQ
Residue
Distance (Å)
VAL202
4.051
MET204
3.524
VAL210
3.984
LEU212
3.723
PHE215
3.362
SER240
3.882
LEU242
3.345
PRO243
1.356
GLU245
1.325
ASP246
2.784
GLN247
3.035
ILE248
3.062
GLY291
3.474
LEU292
4.556
VAL294
3.280
VAL295
3.605
ALA298
3.933
LEU332
3.767
LEU333
1.325
VAL335
1.332
ASP336
3.329
LYS337
3.286
Residue
Distance (Å)
ILE338
3.041
GLU339
4.987
MET376
2.866
ILE377
3.375
GLY378
3.434
ALA379
1.334
HIS381
1.317
ALA382
3.302
SER383
3.318
ARG384
2.832
PHE385
3.067
LEU386
3.291
HIS387
1.360
LYS389
1.349
VAL390
3.304
GLU391
1.327
PRO393
1.327
THR394
3.749
LEU396
3.984
PHE397
3.645
PHE401
4.748
PDB ID: 2H77      Crystal structure of human TR alpha bound T3 in monoclinic space group
Method X-ray diffraction Resolution 2.33 Å Mutation Yes [1]
PDB Sequence
RSLQQRPEPT
161
PEEWDLIHIA
171
TEAHRSTNAQ
181
GSHWKQRRKF
191
LPDDIGQSPI
201

VSMPDGDKVD
211
LEAFSEFTKI
221
ITPAITRVVD
231
FAKKLPMFSE
241
LPCEDQIILL
251

KGCCMEIMSL
261
RAAVRYDPES
271
DTLTLSGEMA
281
VKREQLKNGG
291
LGVVSDAIFE
301

LGKSLSAFNL
311
DDTEVALLQA
321
VLLMSTDRSG
331
LLVDKIEKSQ
342
EAYLLAFEHY
352

VNHRKHNIPH
362
FWPKLLMKVT
372
DLRMIGAHAS
383
RFLHKVEPTE
395
LFPPLFLEVF
405

E
Residue
Distance (Å)
VAL202
3.971
MET204
3.393
VAL210
3.629
LEU212
3.720
PHE215
2.795
LEU242
3.637
PRO243
3.626
ASP246
2.962
GLY290
4.008
GLY291
3.172
LEU292
4.557
VAL294
3.257
VAL295
3.465
ALA298
4.027
LEU332
3.732
LEU333
1.330
VAL335
1.322
ASP336
3.298
LYS337
3.393
ILE338
3.207
Residue
Distance (Å)
MET376
2.956
ILE377
3.398
GLY378
3.454
ALA379
1.330
HIS381
1.311
ALA382
3.340
SER383
3.280
ARG384
2.796
PHE385
3.146
LEU386
3.348
HIS387
1.331
LYS389
1.337
VAL390
3.026
GLU391
1.322
PRO393
1.354
THR394
3.814
LEU396
3.790
PHE397
3.600
PHE401
4.630
PDB ID: 3HZF      Structure of TR-alfa bound to selective thyromimetic GC-1 in C2 space group
Method X-ray diffraction Resolution 2.50 Å Mutation No [2]
PDB Sequence
SHMEEMIRSL
154
QQRPEPTPEE
164
WDLIHIATEA
174
HRSTNAQGSH
184
WKQRRKFLPD
194

DIGQSPIVSM
204
PDGDKVDLEA
214
FSEFTKIITP
224
AITRVVDFAK
234
KLPMFSELPE
245

DQIILLKGCC
255
MEIMSLRAAV
265
RYDPESDTLT
275
LSGEMAVKRE
285
QLKNGGLGVV
295

SDAIFELGKS
305
LSAFNLDDTE
315
VALLQAVLLM
325
STDRSGLLVD
336
KIEKSQEAYL
346

LAFEHYVNHR
356
KHNIPHFWPK
366
LLMKVTDLRM
376
IGAHASRFLH
387
MKVEPTELFP
398

PLFLEVFED
Residue
Distance (Å)
VAL202
4.467
MET204
3.335
VAL210
3.575
LEU212
3.349
PHE215
3.175
LEU242
3.385
PRO243
1.319
GLU245
1.350
ASP246
2.893
GLN247
3.071
ILE248
2.866
VAL294
3.728
VAL295
3.459
ALA298
3.898
LEU332
3.816
LEU333
1.326
VAL335
1.327
ASP336
2.976
LYS337
3.160
ILE338
2.984
Residue
Distance (Å)
GLU339
4.883
ASP373
4.989
MET376
2.878
ILE377
3.437
GLY378
3.573
ALA379
1.326
HIS381
1.331
ALA382
3.374
SER383
3.231
ARG384
2.899
PHE385
4.841
HIS387
4.787
MET388
3.260
LYS389
3.438
VAL390
3.438
GLU391
1.326
PRO393
1.331
THR394
3.595
LEU396
4.120
PHE397
3.715
PDB ID: 3ILZ      Structure of TR-alfa bound to selective thyromimetic GC-1 in P212121 space group
Method X-ray diffraction Resolution 1.85 Å Mutation No [2]
PDB Sequence
GSHMEEMIRS
153
LQQRPEPTPE
163
EWDLIHIATE
173
AHRSTNAQGS
183
HWKQRRKFLP
193

DDIGQSPIVS
203
MPDGDKVDLE
213
AFSEFTKIIT
223
PAITRVVDFA
233
KKLPMFSELP
243

EDQIILLKGC
254
CMEIMSLRAA
264
VRYDPESDTL
274
TLSGEMAVKR
284
EQLKNGGLGV
294

VSDAIFELGK
304
SLSAFNLDDT
314
EVALLQAVLL
324
MSTDRSGLLV
335
DKIEKSQEAY
345

LLAFEHYVNH
355
RKHNIPHFWP
365
KLLMKVTDLR
375
MIGAHASRFL
386
HMKVEPTELF
397

PPLFLEVFED
407
QEV
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CAS or .CAS2 or .CAS3 or :3CAS;style chemicals stick;color identity;select .A:202 or .A:204 or .A:210 or .A:212 or .A:215 or .A:240 or .A:242 or .A:243 or .A:245 or .A:246 or .A:247 or .A:248 or .A:294 or .A:295 or .A:298 or .A:332 or .A:333 or .A:335 or .A:336 or .A:337 or .A:338 or .A:339 or .A:376 or .A:377 or .A:378 or .A:379 or .A:381 or .A:382 or .A:383 or .A:384 or .A:388 or .A:389 or .A:390 or .A:391 or .A:393 or .A:394 or .A:396 or .A:397; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL202
3.922
MET204
3.984
VAL210
4.044
LEU212
3.851
PHE215
3.288
SER240
3.917
LEU242
3.246
PRO243
1.330
GLU245
1.324
ASP246
2.872
GLN247
3.007
ILE248
3.108
VAL294
3.687
VAL295
3.911
ALA298
3.845
LEU332
3.744
LEU333
1.328
VAL335
1.321
ASP336
3.324
Residue
Distance (Å)
LYS337
3.337
ILE338
3.072
GLU339
4.983
MET376
2.978
ILE377
3.250
GLY378
3.379
ALA379
1.326
HIS381
1.330
ALA382
3.292
SER383
3.407
ARG384
3.043
MET388
2.913
LYS389
3.417
VAL390
3.517
GLU391
1.331
PRO393
1.345
THR394
3.736
LEU396
3.936
PHE397
3.637
PDB ID: 4LNW      Crystal structure of TR-alpha bound to T3 in a second site
Method X-ray diffraction Resolution 1.90 Å Mutation No [3]
PDB Sequence
SHMEEMIRSL
154
QQRPEPTPEE
164
WDLIHIATEA
174
HRSTNAQGSH
184
WKQRRKFLPD
194

DIGQSPIVSM
204
PDGDKVDLEA
214
FSEFTKIITP
224
AITRVVDFAK
234
KLPMFSELPE
245

DQIILLKGCC
255
MEIMSLRAAV
265
RYDPESDTLT
275
LSGEMAVKRE
285
QLKNGGLGVV
295

SDAIFELGKS
305
LSAFNLDDTE
315
VALLQAVLLM
325
STDRSGLLVD
336
KIEKSQEAYL
346

LAFEHYVNHR
356
KHNIPHFWPK
366
LLMKVTDLRM
376
IGAHASRFLH
387
MKVEPTELFP
398

PLFLEVFED
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CAS or .CAS2 or .CAS3 or :3CAS;style chemicals stick;color identity;select .A:202 or .A:204 or .A:210 or .A:212 or .A:215 or .A:240 or .A:242 or .A:243 or .A:245 or .A:246 or .A:247 or .A:248 or .A:294 or .A:295 or .A:298 or .A:332 or .A:333 or .A:335 or .A:336 or .A:337 or .A:338 or .A:376 or .A:377 or .A:378 or .A:379 or .A:381 or .A:382 or .A:383 or .A:384 or .A:385 or .A:388 or .A:389 or .A:390 or .A:391 or .A:393 or .A:394 or .A:396 or .A:397; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL202
4.034
MET204
3.989
VAL210
3.794
LEU212
4.441
PHE215
3.221
SER240
3.870
LEU242
3.385
PRO243
1.336
GLU245
1.327
ASP246
2.789
GLN247
3.137
ILE248
3.156
VAL294
3.555
VAL295
3.698
ALA298
3.750
LEU332
3.717
LEU333
1.331
VAL335
1.329
ASP336
3.375
Residue
Distance (Å)
LYS337
3.227
ILE338
2.957
MET376
2.910
ILE377
3.234
GLY378
3.376
ALA379
1.330
HIS381
1.324
ALA382
3.371
SER383
3.397
ARG384
2.961
PHE385
4.955
MET388
2.895
LYS389
3.319
VAL390
3.616
GLU391
1.335
PRO393
1.349
THR394
3.850
LEU396
4.167
PHE397
3.500
PDB ID: 3JZB      Crystal Structure of TR-alfa bound to the selective thyromimetic TRIAC
Method X-ray diffraction Resolution 2.01 Å Mutation No [4]
PDB Sequence
GSHMEEMIRS
153
LQQRPEPTPE
163
EWDLIHIATE
173
AHRSTNAQGS
183
HWKQRRKFLP
193

DDIGQSPIVS
203
MPDGDKVDLE
213
AFSEFTKIIT
223
PAITRVVDFA
233
KKLPMFSELP
243

EDQIILLKGC
254
CMEIMSLRAA
264
VRYDPESDTL
274
TLSGEMAVKR
284
EQLKNGGLGV
294

VSDAIFELGK
304
SLSAFNLDDT
314
EVALLQAVLL
324
MSTDRSGLLV
335
DKIEKSQEAY
345

LLAFEHYVNH
355
RKHNIPHFWP
365
KLLMKVTDLR
375
MIGAHASRFL
386
HMKVEPTELF
397

PPLFLEVFED
407
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CAS or .CAS2 or .CAS3 or :3CAS;style chemicals stick;color identity;select .A:202 or .A:203 or .A:204 or .A:210 or .A:212 or .A:215 or .A:240 or .A:242 or .A:243 or .A:245 or .A:246 or .A:247 or .A:248 or .A:294 or .A:295 or .A:298 or .A:332 or .A:333 or .A:335 or .A:336 or .A:337 or .A:338 or .A:339 or .A:376 or .A:377 or .A:378 or .A:379 or .A:381 or .A:382 or .A:383 or .A:384 or .A:385 or .A:388 or .A:389 or .A:390 or .A:391 or .A:393 or .A:394 or .A:396 or .A:397; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL202
3.448
SER203
4.983
MET204
4.140
VAL210
3.113
LEU212
3.822
PHE215
4.131
SER240
3.953
LEU242
3.432
PRO243
1.344
GLU245
1.330
ASP246
2.779
GLN247
3.075
ILE248
3.030
VAL294
3.485
VAL295
3.697
ALA298
3.945
LEU332
3.767
LEU333
1.327
VAL335
1.328
ASP336
3.297
Residue
Distance (Å)
LYS337
3.303
ILE338
3.008
GLU339
4.968
MET376
2.960
ILE377
3.298
GLY378
3.411
ALA379
1.332
HIS381
1.324
ALA382
3.267
SER383
3.309
ARG384
2.885
PHE385
4.866
MET388
2.859
LYS389
3.402
VAL390
3.596
GLU391
1.332
PRO393
1.335
THR394
3.746
LEU396
4.204
PHE397
3.553
PDB ID: 4LNX      Crystal structure of TR-alpha bound to T4 in a second site
Method X-ray diffraction Resolution 2.05 Å Mutation No [3]
PDB Sequence
SHMEEMIRSL
154
QQRPEPTPEE
164
WDLIHIATEA
174
HRSTNAQGSH
184
WKQRRKFLPD
194

DIGQSPIVSM
204
PDGDKVDLEA
214
FSEFTKIITP
224
AITRVVDFAK
234
KLPMFSELPE
245

DQIILLKGCC
255
MEIMSLRAAV
265
RYDPESDTLT
275
LSGEMAVKRE
285
QLKNGGLGVV
295

SDAIFELGKS
305
LSAFNLDDTE
315
VALLQAVLLM
325
STDRSGLLVD
336
KIEKSQEAYL
346

LAFEHYVNHR
356
KHNIPHFWPK
366
LLMKVTDLRM
376
IGAHASRFLH
387
MKVEPTELFP
398

PLFLEVFED
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CAS or .CAS2 or .CAS3 or :3CAS;style chemicals stick;color identity;select .A:202 or .A:204 or .A:210 or .A:212 or .A:215 or .A:240 or .A:242 or .A:243 or .A:245 or .A:246 or .A:247 or .A:248 or .A:294 or .A:295 or .A:298 or .A:332 or .A:333 or .A:335 or .A:336 or .A:337 or .A:338 or .A:339 or .A:376 or .A:377 or .A:378 or .A:379 or .A:381 or .A:382 or .A:383 or .A:384 or .A:385 or .A:388 or .A:389 or .A:390 or .A:391 or .A:393 or .A:394 or .A:396 or .A:397; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL202
4.118
MET204
4.011
VAL210
4.169
LEU212
3.941
PHE215
3.150
SER240
3.766
LEU242
3.349
PRO243
1.318
GLU245
1.314
ASP246
2.796
GLN247
2.984
ILE248
3.173
VAL294
3.424
VAL295
3.607
ALA298
3.913
LEU332
3.780
LEU333
1.330
VAL335
1.330
ASP336
3.362
LYS337
3.252
Residue
Distance (Å)
ILE338
2.934
GLU339
4.980
MET376
2.853
ILE377
3.370
GLY378
3.425
ALA379
1.331
HIS381
1.330
ALA382
3.333
SER383
3.351
ARG384
2.960
PHE385
4.973
MET388
2.899
LYS389
3.241
VAL390
3.564
GLU391
1.333
PRO393
1.341
THR394
3.797
LEU396
4.208
PHE397
3.742
References  Top
REF 1 Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function. J Mol Biol. 2006 Jul 14;360(3):586-98.
REF 2 Structural basis of GC-1 selectivity for thyroid hormone receptor isoforms. BMC Struct Biol. 2008 Jan 31;8:8.
REF 3 Identification of a new hormone-binding site on the surface of thyroid hormone receptor. Mol Endocrinol. 2014 Apr;28(4):534-45.
REF 4 Gaining ligand selectivity in thyroid hormone receptors via entropy. Proc Natl Acad Sci U S A. 2009 Dec 8;106(49):20717-22.

If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.