5X8Q: Nuclear receptor ROR-gamma
Crystal Structure of the mutant Human ROR gamma Ligand Binding Domain With rockogenin. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Jun 2017.
- Method
- X-ray diffraction
- Resolution
- 2.2 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 8,346
- Mol. weight
- 131.15 kDa
- Ligands
- 82R
- Released
- 7 Jun 2017
Explore 5X8Q in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5X8Q contains 62 α-helices and 16 β-strands across 8 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 14 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-284 | 18 | |
| α-helix | 289-294 | 6 | |
| β-strand | 299 | 1 | 1 |
| α-helix | 302-309 | 8 | |
| α-helix | 313-337 | 25 | |
| α-helix | 346-365 | 20 | |
| α-helix | 366-368 | 3 | |
| β-strand | 369-370 | 2 | 1 |
| β-strand | 375-378 | 4 | 1 |
| β-strand | 381-383 | 3 | 1 |
| α-helix | 385-391 | 7 | |
| α-helix | 394-409 | 16 | |
| α-helix | 414-425 | 12 | |
| α-helix | 436-457 | 22 | |
| α-helix | 460-465 | 6 | |
| α-helix | 466-468 | 3 | |
| α-helix | 470-485 | 16 | |
| α-helix | 487-489 | 3 | |
Chains B, D, F and H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2347-2357 | 11 | |
Chain C: 15 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-284 | 18 | |
| α-helix | 289-294 | 6 | |
| α-helix | 295-297 | 3 | |
| β-strand | 299 | 1 | 2 |
| α-helix | 302-309 | 8 | |
| α-helix | 313-337 | 25 | |
| α-helix | 346-364 | 19 | |
| α-helix | 365-368 | 4 | |
| β-strand | 369-370 | 2 | 2 |
| β-strand | 375-378 | 4 | 2 |
| β-strand | 381-383 | 3 | 2 |
| α-helix | 385-391 | 7 | |
| α-helix | 394-409 | 16 | |
| α-helix | 414-425 | 12 | |
| α-helix | 436-456 | 21 | |
| α-helix | 462-465 | 4 | |
| α-helix | 466-468 | 3 | |
| α-helix | 470-485 | 16 | |
| α-helix | 487-489 | 3 | |
Chain E: 14 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-284 | 18 | |
| α-helix | 289-294 | 6 | |
| β-strand | 299 | 1 | 3 |
| α-helix | 302-309 | 8 | |
| α-helix | 313-337 | 25 | |
| α-helix | 341-343 | 3 | |
| α-helix | 346-364 | 19 | |
| α-helix | 365-368 | 4 | |
| β-strand | 369-370 | 2 | 3 |
| β-strand | 375-378 | 4 | 3 |
| β-strand | 381-383 | 3 | 3 |
| α-helix | 385-391 | 7 | |
| α-helix | 394-409 | 16 | |
| α-helix | 414-425 | 12 | |
| α-helix | 436-456 | 21 | |
| α-helix | 466-468 | 3 | |
| α-helix | 470-486 | 17 | |
| α-helix | 487-489 | 3 | |
Chain G: 15 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-284 | 18 | |
| α-helix | 289-294 | 6 | |
| α-helix | 295-297 | 3 | |
| β-strand | 299 | 1 | 4 |
| α-helix | 302-310 | 9 | |
| α-helix | 313-336 | 24 | |
| α-helix | 346-365 | 20 | |
| α-helix | 366-368 | 3 | |
| β-strand | 369-370 | 2 | 4 |
| β-strand | 375-378 | 4 | 4 |
| β-strand | 381-383 | 3 | 4 |
| α-helix | 385-391 | 7 | |
| α-helix | 394-408 | 15 | |
| α-helix | 414-425 | 12 | |
| α-helix | 436-457 | 22 | |
| α-helix | 460-465 | 6 | |
| α-helix | 466-468 | 3 | |
| α-helix | 470-485 | 16 | |
| α-helix | 487-489 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Nuclear receptor ROR-gamma | A, C, E, G | protein | 258 | Homo sapiens | P51449 (AlphaFold model) |
| Nuclear receptor corepressor 2 | B, D, F, H | protein | 22 | Homo sapiens | Q9Y618 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>5X8Q_1 Nuclear receptor ROR-gamma (chains A, C, E, G)
EAPYASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERC
AHHLTEAIQYVVEFAKRLSGFMELCQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEG
KYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALVLINAHRPGLQEKRKVE
QLQYNLELAFHHHLCKTHRQSILAKLPPAGKLASLCSQHVERLQIFQHLHPIVVQAAFPP
LYKELFSTETESPVGLSK
Sequence of entity 2 (B, D, F, H), FASTA
>5X8Q_2 Nuclear receptor corepressor 2 (chains B, D, F, H)
TNMGLEAIIRKALMGKYDQWEE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 82R | (1R,2S,4S,5'R,6R,7S,8R,9S,10R,12S,13S,16S,18S)-5',7,9,13-tetramethylspiro[5-oxa… | C27 H44 O4 | 4 |
Primary citation
Ternary complex of human ROR gamma ligand-binding domain, inverse agonist and SMRT peptide shows a unique mechanism of corepressor recruitment. Noguchi, M., Nomura, A., Murase, K. et al. Genes Cells (2017) 22:535-551. DOI 10.1111/gtc.12494 · PubMed
Other PDB entries of the same protein (UniProt P51449 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7NPC 1.47 Å, ROR(gamma)t ligand binding domain in complex with allosteric ligand FM156
- 6T4X 1.48 Å, ROR(gamma)t ligand binding domain in complex with 25-hydroxycholesterol and allosteric…
- 5APH 1.54 Å, Ligand complex of RORg LBD
- 6R7K 1.54 Å, Ligand complex of RORg LBD
- 7NP5 1.55 Å, ROR(gamma)t ligand binding domain in complex with allosteric ligand FM216
- 6W9I 1.61 Å, Substituted benzyloxytricyclic compounds as retinoic acid-related orphan receptor gamma…
- 6SAL 1.61 Å, ROR(gamma)t ligand binding domain in complex with allosteric ligand FM26
- 7OFK 1.61 Å, Ligand complex of RORg LBD
- 6T4T 1.62 Å, ROR(gamma)t ligand binding domain in complex with 20-alpha-hydroxycholesterol and…
- 7KXD 1.62 Å, Crystal structure of rar-related orphan receptor C (nhis-RORGT(244-487)-L6-SRC1(678-692))…
- 9N9L 1.64 Å, An RORgt Inverse agonist for treatment of Psoriasis
- 5NTW 1.64 Å, Structural states of RORgt: X-ray elucidation of molecular mechanisms and binding…
Browse structure collections
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