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 T25307 Target Info
Target Name Nuclear receptor ROR-gamma (RORG)
Synonyms Retinoid-related orphan receptor-gamma; RZRG; RORG; RAR-related orphan receptor C; Nuclear receptor subfamily 1 group F member 3; Nuclear receptor RZR-gamma; NR1F3
Target Type Clinical trial Target
Gene Name RORC
Biochemical Class Nuclear hormone receptor
UniProt ID
RORG_HUMAN
Ligand General Information  Top
Ligand Name T0901317 Ligand Info
Canonical SMILES C1=CC=C(C=C1)S(=O)(=O)N(CC(F)(F)F)C2=CC=C(C=C2)C(C(F)(F)F)(C(F)(F)F)O
InChI 1S/C17H12F9NO3S/c18-14(19,20)10-27(31(29,30)13-4-2-1-3-5-13)12-8-6-11(7-9-12)15(28,16(21,22)23)17(24,25)26/h1-9,28H,10H2
InChIKey SGIWFELWJPNFDH-UHFFFAOYSA-N
PubChem Compound ID 447912
Drug Binding Sites of Target  Top
PDB ID: 5EJV      RORy in complex with T090131718 and Coactivator peptide EBI96
Method X-ray diffraction Resolution 2.58 Å Mutation No [1]
PDB Sequence
PYASLTEIEH
272
LVQSVCKSYR
282
ETCQLRLEDL
292
LRQRSNIFSR
302
EEVTGYQRKS
312

MWEMWERCAH
322
HLTEAIQYVV
332
EFAKRLSGFM
342
ELCQNDQIVL
352
LKAGAMEVVL
362

VRMCRAYNAD
372
NRTVFFEGKY
382
GGMELFRALG
392
CSELISSIFD
402
FSHSLSALHF
412

SEDEIALYTA
422
LVLINAHRPG
432
LQEKRKVEQL
442
QYNLELAFHH
452
HLCKTHRQSI
462

LAKLPPKGKL
472
RSLCSQHVER
482
LQIFQHLHPI
492
VVQAAFPPLY
502
KELFS
Residue
Distance (Å)
TRP317
3.627
CYS320
3.500
ALA321
3.588
HIS323
3.765
LEU324
3.325
ALA327
4.017
MET358
4.287
VAL361
3.803
MET365
3.275
VAL376
4.704
PHE377
3.919
Residue
Distance (Å)
PHE378
3.626
PHE388
3.634
LEU391
4.302
CYS393
4.720
LEU396
3.217
ILE397
3.193
ILE400
3.120
PHE401
4.325
HIS479
3.461
TYR502
3.878
PDB ID: 4NB6      Crystal structure of the ligand binding domain of RORC with T0901317
Method X-ray diffraction Resolution 2.85 Å Mutation No [2]
PDB Sequence
SLTEIEHLVQ
254
SVCKSYRETC
264
QLRLEDLLRQ
274
RSNIFSREEV
284
TGYQRKSMWE
294

MWERCAHHLT
304
EAIQYVVEFA
314
KRLSGFMELC
324
QNDQIVLLKA
334
GAMEVVLVRM
344

CRAYNADNRT
354
VFFEGKYGGM
364
ELFRALGCSE
374
LISSIFDFSH
384
SLSALHFSED
394

EIALYTALVL
404
INAHRPGLQE
414
KRKVEQLQYN
424
LELAFHHHLC
434
KTHRQSILAK
444

LPPKGKLRSL
454
CSQHVERLQI
464
F
Residue
Distance (Å)
TRP296
3.244
CYS299
3.295
ALA300
4.901
HIS302
3.478
LEU303
3.284
ALA306
3.721
MET337
3.513
VAL340
3.328
MET344
3.341
VAL355
3.572
PHE356
4.435
Residue
Distance (Å)
PHE357
3.529
PHE367
3.327
LEU370
4.524
LEU375
3.013
ILE376
4.038
ILE379
3.565
PHE380
4.337
HIS458
3.070
VAL459
4.688
LEU462
3.107
PDB ID: 5K3L      Crystal structure of Retinoic acid receptor-related orphan receptor (ROR) gamma ligand binding domain complex with 444
Method X-ray diffraction Resolution 2.75 Å Mutation No [3]
PDB Sequence
ASLTEIEHLV
274
QSVCKSYRET
284
CQLRLEDLLR
294
QRSNIFSREE
304
VTGYQRKSMW
314

EMWERCAHHL
324
TEAIQYVVEF
334
AKRLSGFMEL
344
CQNDQIVLLK
354
AGAMEVVLVR
364

MCRAYNADNR
374
TVFFEGKYGG
384
MELFRALGCS
394
ELISSIFDFS
404
HSLSALHFSE
414

DEIALYTALV
424
LINAHRPGLQ
434
EKRKVEQLQY
444
NLELAFHHHL
454
CKTHRQSILA
464

KLPPKGKLRS
474
LCSQHVERLQ
484
IFQHL
Residue
Distance (Å)
GLN286
4.177
LEU287
4.921
TRP317
3.438
CYS320
2.950
ALA321
4.856
HIS323
2.882
LEU324
3.085
ALA327
3.191
MET358
4.428
VAL361
4.461
MET365
3.308
Residue
Distance (Å)
VAL376
4.240
PHE377
3.159
PHE378
3.990
PHE388
3.452
LEU391
4.690
LEU396
4.959
ILE397
4.617
ILE400
3.431
PHE401
4.982
HIS479
2.528
LEU483
3.583
PDB ID: 5NTQ      Structural states of RORgt: X-ray elucidation of molecular mechanisms and binding interactions for natural and synthetic compounds
Method X-ray diffraction Resolution 2.26 Å Mutation Yes [4]
PDB Sequence
ASLTEIEHLV
274
QSVCKSYRET
284
CQLRLEDLLR
294
QRSNIFSREE
304
VTGYQRKSMW
314

EMWERCAHHL
324
TEAIQYVVEF
334
AKRLSGFMEL
344
CQNDQIVLLK
354
AGAMEVVLVR
364

MCRAYNADNR
374
TVFFEGKYGG
384
MELFRALGCS
394
ELISSIFDFS
404
HSLSALHFSE
414

DEIALYTALV
424
LINAHRPGLQ
434
EKRKVEQLQY
444
NLELAFHHHL
454
SKTHRQSILA
464

KLPPKGKLRS
474
LCSQHVERLQ
484
IFQHLHPIVV
494
QAAF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .444 or .4442 or .4443 or :3444;style chemicals stick;color identity;select .A:317 or .A:320 or .A:321 or .A:323 or .A:324 or .A:327 or .A:358 or .A:361 or .A:362 or .A:365 or .A:376 or .A:377 or .A:378 or .A:388 or .A:391 or .A:396 or .A:397 or .A:400 or .A:401 or .A:479 or .A:483; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP317
3.524
CYS320
3.212
ALA321
4.986
HIS323
3.254
LEU324
3.306
ALA327
3.739
MET358
3.056
VAL361
3.281
LEU362
4.540
MET365
3.545
VAL376
3.432
Residue
Distance (Å)
PHE377
4.096
PHE378
3.615
PHE388
3.526
LEU391
4.272
LEU396
3.436
ILE397
3.819
ILE400
3.515
PHE401
4.641
HIS479
2.805
LEU483
3.425
References  Top
REF 1 Discovery of biaryls as RORGamma inverse agonists by using structure-based design. Bioorg Med Chem Lett. 2016 May 15;26(10):2459-2463.
REF 2 Structure-based design of substituted hexafluoroisopropanol-arylsulfonamides as modulators of RORc. Bioorg Med Chem Lett. 2013 Dec 15;23(24):6604-9.
REF 3 Crystal structure of Retinoic acid receptor-related orphan receptor (ROR) gamma ligand binding domain complex with 444
REF 4 Structural States of RORGammat: X-ray Elucidation of Molecular Mechanisms and Binding Interactions for Natural and Synthetic Compounds. ChemMedChem. 2017 Jul 6;12(13):1014-1021.

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