6G05: Rorgt

Rorgt (264-518;C455S) in complex with inverse agonist "cpd-2" and RIP140 peptide at 1.90A. Determined by X-ray diffraction at 1.9 Å resolution. Released 18 Jul 2018.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 4
Atoms: 4,436
Mol. weight: 65.1 kDa
Ligands: EF5
Released: 18 Jul 2018

Explore 6G05 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6G05 contains 34 α-helices and 8 β-strands across 4 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: 16 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	1
α-helix	302-309	8
α-helix	313-336	24
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	471-489	19
α-helix	491-497	7
α-helix	500-506	7

Chain B: 16 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	267-282	16
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	346-365	20
α-helix	366-368	3
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	394-408	15
α-helix	414-425	12
α-helix	436-455	20
α-helix	459-465	7
α-helix	467-468	2
α-helix	469-489	21
α-helix	491-497	7
α-helix	500-506	7

Chains P and Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	500-505	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nuclear receptor ROR-gamma	A, B	protein	257	Homo sapiens	P51449 (AlphaFold model)
Nuclear receptor-interacting protein 1	P, Q	protein	20	Homo sapiens	P48552 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6G05_1 Nuclear receptor ROR-gamma (chains A, B)
GPYASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCA
HHLTEAIQYVVEFAKRLSGFMELCQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGK
YGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALVLINAHRPGLQEKRKVEQ
LQYNLELAFHHHLSKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPL
YKELFSTETESPVGLSK

Sequence of entity 2 (P, Q), FASTA

>6G05_2 Nuclear receptor-interacting protein 1 (chains P, Q)
NSHQKVTLLQLLLGHKNEEN

Ligands and cofactors

ID	Name	Formula	Copies
EF5	2-(4-ethylsulfonylphenyl)-~{N}-[4-phenyl-5-(phenylcarbonyl)-1,3-thiazol-2-yl]et…	C26 H22 N2 O4 S2	2

Primary citation

Optimizing a Weakly Binding Fragment into a Potent ROR gamma t Inverse Agonist with Efficacy in an in Vivo Inflammation Model. Carcache, D.A., Vulpetti, A., Kallen, J. et al. J Med Chem (2018) 61:6724-6735. DOI 10.1021/acs.jmedchem.8b00529 · 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…

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