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 N-[4-(3-Chlorophenyl)-5-(2-chlorobenzoyl)thiazole-2-yl]-2-[4-(ethylsulfonyl)phenyl]acetamide Ligand Info
Canonical SMILES CCS(=O)(=O)C1=CC=C(C=C1)CC(=O)NC2=NC(=C(S2)C(=O)C3=CC=CC=C3Cl)C4=CC(=CC=C4)Cl
InChI 1S/C26H20Cl2N2O4S2/c1-2-36(33,34)19-12-10-16(11-13-19)14-22(31)29-26-30-23(17-6-5-7-18(27)15-17)25(35-26)24(32)20-8-3-4-9-21(20)28/h3-13,15H,2,14H2,1H3,(H,29,30,31)
InChIKey GRWNPFJXINLSNF-UHFFFAOYSA-N
PubChem Compound ID 56837193
Drug Binding Sites of Target  Top
PDB ID: 5NI5      Ligand complex of RORg LBD
Method X-ray diffraction Resolution 2.30 Å Mutation No [1]
PDB Sequence
ENLYFQGASL
267
TEIEHLVQSV
277
CKSYRETCQL
287
RLEDLLRQRS
297
NIFSREEVTG
307

YQRKSMWEMW
317
ERCAHHLTEA
327
IQYVVEFAKR
337
LSGFMELCQN
347
DQIVLLKAGA
357

MEVVLVRMCR
367
AYNADNRTVF
377
FEGKYGGMEL
387
FRALGCSELI
397
SSIFDFSHSL
407

SALHFSEDEI
417
ALYTALVLIN
427
AHRPGLQEKR
437
KVEQLQYNLE
447
LAFHHHLCKT
457

HRQSILAKLP
467
PKGKLRSLCS
477
QHVERLQIFQ
487
HLHPIVVQAA
497
FPPLYKELFS
507
Residue
Distance (Å)
CYS285
3.222
GLN286
3.078
LEU287
3.148
LEU292
3.814
CYS320
3.409
HIS323
3.554
LEU324
3.726
ALA327
4.248
MET358
3.707
VAL361
4.365
LEU362
4.136
ARG364
3.408
MET365
3.399
Residue
Distance (Å)
ARG367
3.137
ALA368
3.335
TYR369
4.767
VAL376
3.548
PHE377
2.736
PHE378
3.428
GLU379
4.822
PHE388
3.656
LEU391
4.246
ILE397
4.419
ILE400
3.395
PHE401
3.176
SER404
3.820
PDB ID: 5NU1      Structural states of RORgt: X-ray elucidation of molecular mechanisms and binding interactions for natural and synthetic compounds
Method X-ray diffraction Resolution 1.85 Å Mutation Yes [2]
PDB Sequence
YASLTEIEHL
273
VQSVCKSYRE
283
TCQLRLEDLL
293
RQRSNIFSRE
303
EVTGYQRKSM
313

WEMWERCAHH
323
LTEAIQYVVE
333
FAKRLSGFME
343
LCQNDQIVLL
353
KAGAMEVVLV
363

RMCRAYNADN
373
RTVFFEGKYG
383
GMELFRALGC
393
SELISSIFDF
403
SHSLSALHFS
413

EDEIALYTAL
423
VLINAHRPGL
433
QEKRKVEQLQ
443
YNLELAFHHH
453
LSKTHRQSIL
463

AKLPPKGKLR
473
SLCSQHVERL
483
QIFQHLHPIV
493
VQAAFPPLYK
503
ELFST
Residue
Distance (Å)
CYS285
3.116
GLN286
3.232
LEU287
3.112
LEU292
3.885
CYS320
3.303
HIS323
3.345
LEU324
3.483
ALA327
4.710
MET358
4.160
VAL361
4.077
LEU362
4.425
ARG364
3.434
MET365
3.584
ARG367
3.077
Residue
Distance (Å)
ALA368
3.388
TYR369
4.755
VAL376
3.696
PHE377
2.901
PHE378
3.603
GLU379
4.811
PHE388
3.551
LEU391
4.871
LEU396
4.455
ILE397
3.940
ILE400
3.252
PHE401
3.364
SER404
3.536
HIS479
4.718
References  Top
REF 1 Potent and Orally Bioavailable Inverse Agonists of RORGammat Resulting from Structure-Based Design. J Med Chem. 2018 Sep 13;61(17):7796-7813.
REF 2 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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