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 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 (5S)-5-[[4-[2-[[6-(4-methoxyphenoxy)pyrimidin-4-yl]-methyl-amino]ethoxy]phenyl]methyl]-1,3-thiazolidine-2,4-dione Ligand Info
Canonical SMILES CN(CCOC1=CC=C(C=C1)CC2C(=O)NC(=O)S2)C3=CC(=NC=N3)OC4=CC=C(C=C4)OC
InChI 1S/C24H24N4O5S/c1-28(21-14-22(26-15-25-21)33-19-9-7-17(31-2)8-10-19)11-12-32-18-5-3-16(4-6-18)13-20-23(29)27-24(30)34-20/h3-10,14-15,20H,11-13H2,1-2H3,(H,27,29,30)/t20-/m0/s1
InChIKey CHHXEZSCHQVSRE-FQEVSTJZSA-N
PubChem Compound ID 76965111
Drug Binding Sites of Target  Top
PDB ID: 5Y2T      Structure of PPARgamma ligand binding domain - lobeglitazone complex
Method X-ray diffraction Resolution 1.70 Å Mutation No [1]
PDB Sequence
ESADLRALAK
216
HLYDSYIKSF
226
PLTKAKARAI
236
LTGKTTDKSP
246
FVIYDMNSLM
256

MGEDKIKQSK
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
L
Residue
Distance (Å)
ILE249
4.199
LEU255
3.835
GLY258
3.688
GLU259
3.947
ILE262
4.632
ARG280
3.767
ILE281
3.707
PHE282
3.144
GLY284
3.548
CYS285
3.399
GLN286
3.765
ARG288
4.235
SER289
2.636
HIS323
2.765
Residue
Distance (Å)
ILE326
4.214
TYR327
3.520
LEU330
3.868
VAL339
4.154
LEU340
4.504
ILE341
3.488
MET348
3.479
LEU353
4.133
MET364
3.622
LYS367
4.766
HIS449
2.965
LEU453
3.702
LEU469
4.019
TYR473
2.889
PDB ID: 5YCN      Human PPARgamma ligand binding domain complexed with Lobeglitazone
Method X-ray diffraction Resolution 2.15 Å Mutation No [2]
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
Residue
Distance (Å)
ILE249
4.095
LEU255
3.486
GLU259
4.262
ARG280
3.515
ILE281
3.567
PHE282
3.194
GLY284
3.880
CYS285
3.388
GLN286
4.111
ARG288
4.583
SER289
2.726
HIS323
2.780
ILE326
4.211
TYR327
3.582
Residue
Distance (Å)
LEU330
3.881
VAL339
3.962
LEU340
4.478
ILE341
3.560
MET348
3.820
LEU353
4.251
PHE363
4.274
MET364
3.633
LYS367
4.921
HIS449
2.956
LEU453
3.556
LEU465
4.956
LEU469
3.795
TYR473
2.903
References  Top
REF 1 Structures of PPARGamma complexed with lobeglitazone and pioglitazone reveal key determinants for the recognition of antidiabetic drugs. Sci Rep. 2017 Dec 4;7(1):16837.
REF 2 Structural Basis for the Enhanced Anti-Diabetic Efficacy of Lobeglitazone on PPARGamma. Sci Rep. 2018 Jan 8;8(1):31.

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