6R7K: Ligand complex of RORg LBD

Ligand complex of RORg LBD. Determined by X-ray diffraction at 1.54 Å resolution. Released 3 Jul 2019.

Method: X-ray diffraction
Resolution: 1.54 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,501
Mol. weight: 35.45 kDa
Ligands: JUH
Released: 3 Jul 2019

Explore 6R7K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6R7K contains 19 α-helices and 4 β-strands across 2 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: 18 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	260-262	3
α-helix	267-282	16
α-helix	289-294	6
α-helix	295-297	3
β-strand	299	1	1
α-helix	302-310	9
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	1
β-strand	375-378	4	1
β-strand	381-383	3	1
α-helix	385-391	7
α-helix	394-408	15
α-helix	414-425	12
α-helix	436-456	21
α-helix	460-465	6
α-helix	467-468	2
α-helix	469-489	21
α-helix	491-497	7
α-helix	500-506	7

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	690-695	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nuclear receptor ROR-gamma	A	protein	283	Homo sapiens	P51449 (AlphaFold model)
SRC2 peptide	C	protein	15	Homo sapiens	Q15596 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6R7K_1 Nuclear receptor ROR-gamma (chains A)
MHNHNHNHNHNHNGGENLYFQGASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSR
EEVTGYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMELCQNDQIVLLKAGAMEVVL
VRMCRAYNADNRTVFFEGKYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTA
LVLINAHRPGLQEKRKVEQLQYNLELAFHHHLCKTHRQSILAKLPPKGKLRSLCSQHVER
LQIFQHLHPIVVQAAFPPLYKELFSGGGKEKHKILHRLLQDSS

Sequence of entity 2 (C), FASTA

>6R7K_2 SRC2 peptide (chains C)
KEKHKILHRLLQDSS

Ligands and cofactors

ID	Name	Formula	Copies
JUH	(2~{R})-2-(4-ethylsulfonylphenyl)-~{N}-[4-[1,1,1,3,3,3-hexakis(fluoranyl)-2-oxi…	C27 H24 F6 N2 O5 S	1

Water and common crystallization additives (NA, DMS) are not listed.

Primary citation

Discovery of Potent and Orally Bioavailable Inverse Agonists of the Retinoic Acid Receptor-Related Orphan Receptor C2. von Berg, S., Xue, Y., Collins, M. et al. ACS Med Chem Lett (2019) 10:972-977. DOI 10.1021/acsmedchemlett.9b00158 · 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
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…
6G07 1.66 Å, Rorgt (264-518;C455S) in complex with inverse agonist "cpd-9" and RIP140 peptide at 1.66A

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