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 T58921 Target Info
Target Name Peroxisome proliferator-activated receptor gamma (PPAR-gamma)
Synonyms PPAR-gamma; Nuclear receptor subfamily 1 group C member 3; NR1C3
Target Type Successful Target
Gene Name PPARG
Biochemical Class Nuclear hormone receptor
UniProt ID
PPARG_HUMAN
Ligand General Information  Top
Ligand Name 2,4-Thiazolidiinedione, 5-[[4-[2-(methyl-2-pyridinylamino)ethoxy]phenyl]methyl]-(9CL) Ligand Info
Canonical SMILES CN(CCOC1=CC=C(C=C1)CC2C(=O)NC(=O)S2)C3=CC=CC=N3
InChI 1S/C18H19N3O3S/c1-21(16-4-2-3-9-19-16)10-11-24-14-7-5-13(6-8-14)12-15-17(22)20-18(23)25-15/h2-9,15H,10-12H2,1H3,(H,20,22,23)/t15-/m0/s1
InChIKey YASAKCUCGLMORW-HNNXBMFYSA-N
PubChem Compound ID 445655
Drug Binding Sites of Target  Top
PDB ID: 3DZY      Intact PPAR gamma - RXR alpha Nuclear Receptor Complex on DNA bound with Rosiglitazone, 9-cis Retinoic Acid and NCOA2 Peptide
Method X-ray diffraction Resolution 3.10 Å Mutation No [1]
PDB Sequence
AIECRVCGDK
117
ASGFHYGVHA
127
CEGCKGFFRR
137
TIRLKLIYDR
147
CDLNCRIHKK
157

SRNKCQYCRF
167
QKCLAVGMSH
177
NAIRFGRMPQ
187
AEKEKLLAEI
197
SSDIDQLNPE
207

SADLRALAKH
217
LYDSYIKSFP
227
LTKAKARAIL
237
TGKTTDKSPF
247
VIYDMNSLMM
257

GEEVAIRIFQ
283
GCQFRSVEAV
293
QEITEYAKSI
303
PGFVNLDLND
313
QVTLLKYGVH
323

EIIYTMLASL
333
MNKDGVLISE
343
GQGFMTREFL
353
KSLRKPFGDF
363
MEPKFEFAVK
373

FNALELDDSD
383
LAIFIAVIIL
393
SGDRPGLLNV
403
KPIEDIQDNL
413
LQALELQLKL
423

NHPESSQLFA
433
KLLQKMTDLR
443
QIVTEHVQLL
453
QVIKKTETDM
463
SLHPLLQEIY
473

KDLY
Residue
Distance (Å)
ILE281
3.627
PHE282
3.614
GLY284
4.051
CYS285
3.698
GLN286
3.592
ARG288
3.399
SER289
2.923
HIS323
3.012
ILE326
4.319
TYR327
3.903
LEU330
3.339
VAL339
3.860
Residue
Distance (Å)
LEU340
4.594
ILE341
3.683
SER342
4.894
MET348
4.149
LEU353
3.631
PHE363
4.209
MET364
3.418
LYS367
4.599
HIS449
3.595
LEU453
3.845
LEU469
4.096
TYR473
2.925
PDB ID: 4XLD      Crystal structure of the human PPARg-LBD/rosiglitazone complex obtained by dry co-crystallization and in situ diffraction
Method X-ray diffraction Resolution 2.45 Å Mutation No [2]
PDB Sequence
MQLNPESADL
211
RALAKHLYDS
221
YIKSFPLTKA
231
KARAILTGKT
241
SPFVIYDMNS
254

LMMGEDKIKF
264
KEVAIRIFQG
284
CQFRSVEAVQ
294
EITEYAKSIP
304
GFVNLDLNDQ
314

VTLLKYGVHE
324
IIYTMLASLM
334
NKDGVLISEG
344
QGFMTREFLK
354
SLRKPFGDFM
364

EPKFEFAVKF
374
NALELDDSDL
384
AIFIAVIILS
394
GDRPGLLNVK
404
PIEDIQDNLL
414

QALELQLKLN
424
HPESSQLFAK
434
LLQKMTDLRQ
444
IVTEHVQLLQ
454
VIKKTETDMS
464

LHPLLQEIYK
474
DLY
Residue
Distance (Å)
ILE281
3.843
PHE282
3.318
GLY284
3.809
CYS285
3.513
GLN286
4.379
ARG288
4.362
SER289
2.379
HIS323
2.659
ILE326
4.318
TYR327
3.375
LEU330
3.815
Residue
Distance (Å)
VAL339
4.198
LEU340
4.411
ILE341
3.593
MET348
4.060
LEU353
4.720
PHE363
3.530
MET364
3.458
HIS449
2.888
LEU453
4.058
LEU469
3.957
TYR473
2.428
PDB ID: 4O8F      Crystal Structure of the complex between PPARgamma mutant R357A and rosiglitazone
Method X-ray diffraction Resolution 2.60 Å Mutation Yes [3]
PDB Sequence
ESADLRALAK
216
HLYDSYIKSF
226
PLTKAKARAI
236
LTGKTSPFVI
249
YDMNSLMMGE
259

DTPLEVAIRI
281
FQGCQFRSVE
291
AVQEITEYAK
301
SIPGFVNLDL
311
NDQVTLLKYG
321

VHEIIYTMLA
331
SLMNKDGVLI
341
SEGQGFMTRE
351
FLKSLAKPFG
361
DFMEPKFEFA
371

VKFNALELDD
381
SDLAIFIAVI
391
ILSGDRPGLL
401
NVKPIEDIQD
411
NLLQALELQL
421

KLNHPESSQL
431
FAKLLQKMTD
441
LRQIVTEHVQ
451
LLQVIKKTEL
465
HPLLQEIYKD
475

LY
Residue
Distance (Å)
ILE281
4.097
PHE282
3.328
GLY284
3.783
CYS285
3.281
GLN286
4.104
ARG288
2.896
SER289
2.587
HIS323
2.961
ILE326
4.043
TYR327
3.779
LEU330
3.992
VAL339
3.484
Residue
Distance (Å)
LEU340
4.720
ILE341
3.418
MET348
3.755
LEU353
3.615
PHE363
4.724
MET364
3.787
HIS449
2.885
LEU453
3.790
LEU465
4.741
LEU469
3.759
TYR473
2.885
PDB ID: 5YCP      Human PPARgamma ligand binding domain complexed with Rosiglitazone
Method X-ray diffraction Resolution 2.00 Å Mutation No [4]
PDB Sequence
LNPESADLRA
213
LAKHLYDSYI
223
KSFPLTKAKA
233
RAILTGKTTD
243
KSPFVIYDMN
253

SLMMGEDKQS
274
KEVAIRIFQG
284
CQFRSVEAVQ
294
EITEYAKSIP
304
GFVNLDLNDQ
314

VTLLKYGVHE
324
IIYTMLASLM
334
NKDGVLISEG
344
QGFMTREFLK
354
SLRKPFGDFM
364

EPKFEFAVKF
374
NALELDDSDL
384
AIFIAVIILS
394
GDRPGLLNVK
404
PIEDIQDNLL
414

QALELQLKLN
424
HPESSQLFAK
434
LLQKMTDLRQ
444
IVTEHVQLLQ
454
VIKKTETDMS
464

LHPLLQEIYK
474
DLY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:281 or .A:282 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:327 or .A:330 or .A:339 or .A:340 or .A:341 or .A:348 or .A:353 or .A:363 or .A:364 or .A:449 or .A:453 or .A:469 or .A:473; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE281
3.803
PHE282
3.208
GLY284
3.903
CYS285
3.440
GLN286
4.108
ARG288
4.415
SER289
2.703
HIS323
2.715
ILE326
4.219
TYR327
3.567
LEU330
3.816
Residue
Distance (Å)
VAL339
3.960
LEU340
4.367
ILE341
3.457
MET348
3.954
LEU353
4.311
PHE363
4.353
MET364
3.570
HIS449
2.884
LEU453
3.669
LEU469
3.876
TYR473
2.812
PDB ID: 7AWC      Crystal structure of Peroxisome proliferator-activated receptor gamma (PPARG)in complex with rosiglitazone
Method X-ray diffraction Resolution 1.74 Å Mutation No [5]
PDB Sequence
SMQLNPESAD
210
LRALAKHLYD
220
SYIKSFPLTK
230
AKARAILTGK
240
TTDKSPFVIY
250

DMNSLMMGED
260
KIKLQEQSKE
276
VAIRIFQGCQ
286
FRSVEAVQEI
296
TEYAKSIPGF
306

VNLDLNDQVT
316
LLKYGVHEII
326
YTMLASLMNK
336
DGVLISEGQG
346
FMTREFLKSL
356

RKPFGDFMEP
366
KFEFAVKFNA
376
LELDDSDLAI
386
FIAVIILSGD
396
RPGLLNVKPI
406

EDIQDNLLQA
416
LELQLKLNHP
426
ESSQLFAKLL
436
QKMTDLRQIV
446
TEHVQLLQVI
456

KKTETDMSLH
466
PLLQEIYKDL
476
Y
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:281 or .A:282 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:327 or .A:330 or .A:339 or .A:340 or .A:341 or .A:348 or .A:353 or .A:363 or .A:364 or .A:449 or .A:453 or .A:465 or .A:469 or .A:473; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE281
3.868
PHE282
3.325
GLY284
3.932
CYS285
3.444
GLN286
4.159
ARG288
4.131
SER289
2.755
HIS323
2.720
ILE326
4.170
TYR327
3.595
LEU330
3.784
VAL339
3.866
Residue
Distance (Å)
LEU340
4.364
ILE341
3.512
MET348
3.984
LEU353
4.235
PHE363
4.295
MET364
3.445
HIS449
2.793
LEU453
3.528
LEU465
4.850
LEU469
3.886
TYR473
2.725
PDB ID: 6MD4      Crystal Structure of Human PPARgamma Ligand Binding Domain in Complex with Rosiglitazone and Oleic acid
Method X-ray diffraction Resolution 2.24 Å Mutation No [6]
PDB Sequence
ESADLRALAK
216
HLYDSYIKSF
226
PLTKAKARAI
236
LTGKTTDKSP
246
FVIYDMNSLM
256

MGEDKIKFKE
276
VAIRIFQGCQ
286
FRSVEAVQEI
296
TEYAKSIPGF
306
VNLDLNDQVT
316

LLKYGVHEII
326
YTMLASLMNK
336
DGVLISEGQG
346
FMTREFLKSL
356
RKPFGDFMEP
366

KFEFAVKFNA
376
LELDDSDLAI
386
FIAVIILSGD
396
RPGLLNVKPI
406
EDIQDNLLQA
416

LELQLKLNHP
426
ESSQLFAKLL
436
QKMTDLRQIV
446
TEHVQLLQVI
456
KKTETDMSLH
466

PLLQEIYK
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:281 or .A:282 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:327 or .A:330 or .A:339 or .A:340 or .A:341 or .A:348 or .A:353 or .A:364 or .A:367 or .A:449 or .A:453 or .A:465 or .A:469 or .A:473; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE281
3.998
PHE282
3.017
GLY284
3.817
CYS285
3.391
GLN286
3.212
ARG288
4.274
SER289
2.743
HIS323
2.589
ILE326
4.026
TYR327
3.467
LEU330
3.702
VAL339
4.082
Residue
Distance (Å)
LEU340
4.459
ILE341
3.743
MET348
4.011
LEU353
4.450
MET364
3.381
LYS367
4.787
HIS449
3.475
LEU453
4.285
LEU465
4.437
LEU469
4.226
TYR473
2.750
PDB ID: 3CS8      Structural and Biochemical Basis for the Binding Selectivity of PPARg to PGC-1a
Method X-ray diffraction Resolution 2.30 Å Mutation No [7]
PDB Sequence
RGGSPESADL
211
RALAKHLYDS
221
YIKSFPLTKA
231
KARAILTGKT
241
TDKSPFVIYD
251

MNSLMMGEDK
261
IPLQEQSKEV
277
AIRIFQGCQF
287
RSVEAVQEIT
297
EYAKSIPGFV
307

NLDLNDQVTL
317
LKYGVHEIIY
327
TMLASLMNKD
337
GVLISEGQGF
347
MTREFLKSLR
357

KPFGDFMEPK
367
FEFAVKFNAL
377
ELDDSDLAIF
387
IAVIILSGDR
397
PGLLNVKPIE
407

DIQDNLLQAL
417
ELQLKLNHPE
427
SSQLFAKLLQ
437
KMTDLRQIVT
447
EHVQLLQVIK
457

KTETDMSLHP
467
LLQEIYKDL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:261 or .A:281 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:330 or .A:341 or .A:342 or .A:348 or .A:353 or .A:363 or .A:364 or .A:367 or .A:449 or .A:453 or .A:465 or .A:469 or .A:473; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS261
4.596
ILE281
3.591
GLY284
3.722
CYS285
3.272
GLN286
3.540
ARG288
4.300
SER289
2.938
HIS323
3.706
ILE326
3.877
LEU330
3.704
ILE341
3.529
Residue
Distance (Å)
SER342
4.556
MET348
4.254
LEU353
4.464
PHE363
4.943
MET364
2.812
LYS367
3.135
HIS449
2.983
LEU453
3.079
LEU465
4.770
LEU469
3.341
TYR473
2.871
PDB ID: 6ONJ      Crystal structure of PPARgamma ligand binding domain in complex with TRAP220 peptide and agonist rosiglitazone
Method X-ray diffraction Resolution 2.30 Å Mutation No [8]
PDB Sequence
ESADLRALAK
216
HLYDSYIKSF
226
PLTKAKARAI
236
LTSPFVIYDM
252
NSLMMGEDKI
262

KHITPLEVAI
279
RIFQGCQFRS
289
VEAVQEITEY
299
AKSIPGFVNL
309
DLNDQVTLLK
319

YGVHEIIYTM
329
LASLMNKDGV
339
LISEGQGFMT
349
REFLKSLRKP
359
FGDFMEPKFE
369

FAVKFNALEL
379
DDSDLAIFIA
389
VIILSGDRPG
399
LLNVKPIEDI
409
QDNLLQALEL
419

QLKLNHPESS
429
QLFAKLLQKM
439
TDLRQIVTEH
449
VQLLQVIKKT
459
ETDMSLHPLL
469

QEIYKDLY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:281 or .A:282 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:327 or .A:330 or .A:339 or .A:340 or .A:341 or .A:342 or .A:348 or .A:353 or .A:363 or .A:364 or .A:449 or .A:453 or .A:469 or .A:473; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE281
3.526
PHE282
3.050
GLY284
3.438
CYS285
3.428
GLN286
4.468
ARG288
4.268
SER289
2.492
HIS323
2.809
ILE326
4.182
TYR327
3.801
LEU330
3.623
VAL339
3.546
Residue
Distance (Å)
LEU340
4.009
ILE341
3.401
SER342
4.795
MET348
3.792
LEU353
4.389
PHE363
3.722
MET364
3.550
HIS449
2.696
LEU453
3.401
LEU469
3.679
TYR473
2.443
PDB ID: 4EMA      Human peroxisome proliferator-activated receptor gamma in complex with rosiglitazone
Method X-ray diffraction Resolution 2.54 Å Mutation No [9]
PDB Sequence
ESADLRALAK
216
HLYDSYIKSF
226
PLTKAKARAI
236
LTGKTTDKSP
246
FVIYDMNSLM
256

MGEDEVAIRI
281
FQGCQFRSVE
291
AVQEITEYAK
301
SIPGFVNLDL
311
NDQVTLLKYG
321

VHEIIYTMLA
331
SLMNKDGVLI
341
SEGQGFMTRE
351
FLKSLRKPFG
361
DFMEPKFEFA
371

VKFNALELDD
381
SDLAIFIAVI
391
ILSGDRPGLL
401
NVKPIEDIQD
411
NLLQALELQL
421

KLNHPESSQL
431
FAKLLQKMTD
441
LRQIVTEHVQ
451
LLQVIKKTET
461
DMSLHPLLQE
471

IYKDLY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:281 or .A:282 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:327 or .A:330 or .A:339 or .A:340 or .A:341 or .A:348 or .A:353 or .A:363 or .A:364 or .A:367 or .A:449 or .A:453 or .A:465 or .A:469 or .A:473; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE281
3.689
PHE282
3.891
GLY284
3.594
CYS285
3.450
GLN286
4.332
ARG288
4.305
SER289
2.575
HIS323
2.892
ILE326
4.135
TYR327
3.654
LEU330
3.727
VAL339
3.973
Residue
Distance (Å)
LEU340
4.559
ILE341
3.840
MET348
3.927
LEU353
4.233
PHE363
4.027
MET364
3.508
LYS367
4.948
HIS449
2.707
LEU453
3.763
LEU465
4.560
LEU469
3.777
TYR473
2.593
PDB ID: 5JI0      PPARgamma-RXRalpha(S427F) heterodimer in complex with SRC-1, rosiglitazone, and 9-cis-retanoic acid
Method X-ray diffraction Resolution 1.98 Å Mutation Yes [10]
PDB Sequence
GPESADLRAL
214
AKHLYDSYIK
224
SFPLTKAKAR
234
AILTGKTTDK
244
SPFVIYDMNS
254

LMMGEDKIIT
268
PLQEQSKEVA
278
IRIFQGCQFR
288
SVEAVQEITE
298
YAKSIPGFVN
308

LDLNDQVTLL
318
KYGVHEIIYT
328
MLASLMNKDG
338
VLISEGQGFM
348
TREFLKSLRK
358

PFGDFMEPKF
368
EFAVKFNALE
378
LDDSDLAIFI
388
AVIILSGDRP
398
GLLNVKPIED
408

IQDNLLQALE
418
LQLKLNHPES
428
SQLFAKLLQK
438
MTDLRQIVTE
448
HVQLLQVIKK
458

TETDMSLHPL
468
LQEIYKDLY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .D:262 or .D:281 or .D:282 or .D:284 or .D:285 or .D:286 or .D:288 or .D:289 or .D:323 or .D:326 or .D:327 or .D:330 or .D:339 or .D:340 or .D:341 or .D:348 or .D:353 or .D:363 or .D:364 or .D:449 or .D:453 or .D:469 or .D:473; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE262
4.759
ILE281
3.817
PHE282
3.540
GLY284
3.736
CYS285
3.417
GLN286
3.424
ARG288
4.200
SER289
2.916
HIS323
2.793
ILE326
4.088
TYR327
3.615
LEU330
3.733
Residue
Distance (Å)
VAL339
3.800
LEU340
4.023
ILE341
3.423
MET348
4.205
LEU353
4.247
PHE363
4.545
MET364
3.668
HIS449
2.764
LEU453
3.564
LEU469
4.186
TYR473
2.756
PDB ID: 1ZGY      Structural and Biochemical Basis for Selective Repression of the Orphan Nuclear Receptor LRH-1 by SHP
Method X-ray diffraction Resolution 1.80 Å Mutation No [11]
PDB Sequence
PESADLRALA
215
KHLYDSYIKS
225
FPLTKAKARA
235
ILTGKTTDKS
245
PFVIYDMNSL
255

MMGEDKIKFK
265
HITPLQEQSK
275
EVAIRIFQGC
285
QFRSVEAVQE
295
ITEYAKSIPG
305

FVNLDLNDQV
315
TLLKYGVHEI
325
IYTMLASLMN
335
KDGVLISEGQ
345
GFMTREFLKS
355

LRKPFGDFME
365
PKFEFAVKFN
375
ALELDDSDLA
385
IFIAVIILSG
395
DRPGLLNVKP
405

IEDIQDNLLQ
415
ALELQLKLNH
425
PESSQLFAKL
435
LQKMTDLRQI
445
VTEHVQLLQV
455

IKKTETDMSL
465
HPLLQEIYKD
475
LY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:281 or .A:282 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:327 or .A:330 or .A:339 or .A:340 or .A:341 or .A:348 or .A:353 or .A:363 or .A:364 or .A:449 or .A:453 or .A:469 or .A:473; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE281
3.754
PHE282
3.313
GLY284
3.654
CYS285
3.676
GLN286
4.420
ARG288
4.074
SER289
2.956
HIS323
2.838
ILE326
3.893
TYR327
3.572
LEU330
3.664
Residue
Distance (Å)
VAL339
4.033
LEU340
4.452
ILE341
3.520
MET348
3.911
LEU353
3.918
PHE363
4.869
MET364
3.496
HIS449
3.027
LEU453
3.577
LEU469
3.539
TYR473
2.858
PDB ID: 1FM6      THE 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE HETERODIMER OF THE HUMAN RXRALPHA AND PPARGAMMA LIGAND BINDING DOMAINS RESPECTIVELY BOUND WITH 9-CIS RETINOIC ACID AND ROSIGLITAZONE AND CO-ACTIVATOR PEPTIDES.
Method X-ray diffraction Resolution 2.10 Å Mutation No [12]
PDB Sequence
PESADLRALA
215
KHLYDSYIKS
225
FPLTKAKARA
235
ILTGKTTDKS
245
PFVIYDMNSL
255

MMGEDKIKFK
265
HITPLQEQSK
275
EVAIRIFQGC
285
QFRSVEAVQE
295
ITEYAKSIPG
305

FVNLDLNDQV
315
TLLKYGVHEI
325
IYTMLASLMN
335
KDGVLISEGQ
345
GFMTREFLKS
355

LRKPFGDFME
365
PKFEFAVKFN
375
ALELDDSDLA
385
IFIAVIILSG
395
DRPGLLNVKP
405

IEDIQDNLLQ
415
ALELQLKLNH
425
PESSQLFAKL
435
LQKMTDLRQI
445
VTEHVQLLQV
455

IKKTETDMSL
465
HPLLQEIYKD
475
LY
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .D:280 or .D:281 or .D:282 or .D:284 or .D:285 or .D:286 or .D:288 or .D:289 or .D:323 or .D:326 or .D:327 or .D:330 or .D:339 or .D:340 or .D:341 or .D:348 or .D:353 or .D:363 or .D:364 or .D:449 or .D:453 or .D:465 or .D:469 or .D:473; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ARG280
4.993
ILE281
3.668
PHE282
3.353
GLY284
3.676
CYS285
3.382
GLN286
4.120
ARG288
4.182
SER289
2.950
HIS323
2.666
ILE326
4.007
TYR327
3.813
LEU330
3.505
Residue
Distance (Å)
VAL339
3.986
LEU340
4.610
ILE341
3.573
MET348
3.572
LEU353
3.948
PHE363
4.644
MET364
3.436
HIS449
2.844
LEU453
3.467
LEU465
4.878
LEU469
3.499
TYR473
2.821
PDB ID: 2PRG      LIGAND-BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA
Method X-ray diffraction Resolution 2.30 Å Mutation No [13]
PDB Sequence
ESADLRALAK
216
HLYDSYIKSF
226
PLTKAKARAI
236
LTGKTTDKSP
246
FVIYDMNSLM
256

MGEDKIKFKH
266
ITPLQEQSKE
276
VAIRIFQGCQ
286
FRSVEAVQEI
296
TEYAKSIPGF
306

VNLDLNDQVT
316
LLKYGVHEII
326
YTMLASLMNK
336
DGVLISEGQG
346
FMTREFLKSL
356

RKPFGDFMEP
366
KFEFAVKFNA
376
LELDDSDLAI
386
FIAVIILSGD
396
RPGLLNVKPI
406

EDIQDNLLQA
416
LELQLKLNHP
426
ESSQLFAKLL
436
QKMTDLRQIV
446
TEHVQLLQVI
456

KKTETDMSLH
466
PLLQEIYKDL
476
Y
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .BRL or .BRL2 or .BRL3 or :3BRL;style chemicals stick;color identity;select .A:281 or .A:282 or .A:284 or .A:285 or .A:286 or .A:288 or .A:289 or .A:323 or .A:326 or .A:327 or .A:330 or .A:339 or .A:340 or .A:341 or .A:342 or .A:348 or .A:363 or .A:364 or .A:449 or .A:453 or .A:469 or .A:473; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE281
3.718
PHE282
3.451
GLY284
3.651
CYS285
3.620
GLN286
2.912
ARG288
4.250
SER289
2.770
HIS323
2.772
ILE326
4.045
TYR327
3.663
LEU330
3.718
Residue
Distance (Å)
VAL339
4.122
LEU340
3.956
ILE341
3.349
SER342
4.706
MET348
3.827
PHE363
4.540
MET364
3.436
HIS449
2.974
LEU453
3.764
LEU469
4.417
TYR473
3.041
References  Top
REF 1 Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. Nature. 2008 Nov 20;456(7220):350-6.
REF 2 Combining 'dry' co-crystallization and in situ diffraction to facilitate ligand screening by X-ray crystallography. Acta Crystallogr D Biol Crystallogr. 2015 Aug;71(Pt 8):1777-87.
REF 3 Structural basis of the transactivation deficiency of the human PPARGamma F360L mutant associated with familial partial lipodystrophy. Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):1965-76.
REF 4 Structural Basis for the Enhanced Anti-Diabetic Efficacy of Lobeglitazone on PPARGamma. Sci Rep. 2018 Jan 8;8(1):31.
REF 5 Endogenous vitamin E metabolites mediate allosteric PPARGamma activation with unprecedented co-regulatory interactions. Cell Chem Biol. 2021 Oct 21;28(10):1489-1500.e8.
REF 6 Cooperative cobinding of synthetic and natural ligands to the nuclear receptor PPARGamma. Elife. 2018 Dec 21;7:e43320.
REF 7 Structural and biochemical basis for the binding selectivity of peroxisome proliferator-activated receptor gamma to PGC-1alpha. J Biol Chem. 2008 Jul 4;283(27):19132-9.
REF 8 A molecular switch regulating transcriptional repression and activation of PPARGamma. Nat Commun. 2020 Feb 19;11(1):956.
REF 9 Medium chain fatty acids are selective peroxisome proliferator activated receptor (PPAR) Gamma activators and pan-PPAR partial agonists. PLoS One. 2012;7(5):e36297.
REF 10 PPARgamma-RXRalpha(S427F) heterodimer in complex with SRC-1, rosiglitazone, and 9-cis-retanoic acid
REF 11 Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner. Proc Natl Acad Sci U S A. 2005 Jul 5;102(27):9505-10.
REF 12 Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell. 2000 Mar;5(3):545-55.
REF 13 Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998 Sep 10;395(6698):137-43.

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