5NTI: Nuclear receptor ROR-gamma
Structural states of RORgt: X-ray elucidation of molecular mechanisms and binding interactions for natural and synthetic compounds. Determined by X-ray diffraction at 2.4 Å resolution. Released 21 Jun 2017.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 8,940
- Mol. weight
- 130.1 kDa
- Ligands
- C3S
- Released
- 21 Jun 2017
Explore 5NTI in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5NTI contains 68 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: 15 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-283 | 17 | |
| α-helix | 289-294 | 6 | |
| β-strand | 299 | 1 | 1 |
| 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 | 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 B: 17 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-283 | 17 | |
| 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 | 341-343 | 3 | |
| α-helix | 346-364 | 19 | |
| α-helix | 365-367 | 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 | 436-456 | 21 | |
| α-helix | 460-463 | 4 | |
| α-helix | 467-468 | 2 | |
| α-helix | 469-489 | 21 | |
| α-helix | 491-496 | 6 | |
| α-helix | 500-506 | 7 | |
Chain C: 16 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 267-283 | 17 | |
| α-helix | 289-294 | 6 | |
| β-strand | 299 | 1 | 3 |
| α-helix | 300-301 | 2 | |
| α-helix | 302-310 | 9 | |
| α-helix | 313-336 | 24 | |
| α-helix | 346-364 | 19 | |
| α-helix | 365-367 | 3 | |
| 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 | 459-465 | 7 | |
| α-helix | 467-468 | 2 | |
| α-helix | 469-489 | 21 | |
| α-helix | 491-497 | 7 | |
| α-helix | 500-506 | 7 | |
Chain D: 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 | 4 |
| α-helix | 302-310 | 9 | |
| α-helix | 313-336 | 24 | |
| α-helix | 346-364 | 19 | |
| α-helix | 365-367 | 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 | 436-455 | 20 | |
| α-helix | 460-463 | 4 | |
| α-helix | 467-468 | 2 | |
| α-helix | 469-489 | 21 | |
| α-helix | 491-497 | 7 | |
| α-helix | 500-506 | 7 | |
Chains P, Q, R and S: 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, C, D | protein | 257 | Homo sapiens | P51449 (AlphaFold model) |
| Asn-ser-his-gln-lys-val-thr-leu-leu-gln-leu-leu-leu-gly-his-lys-asn-glu-glu-asn | P, Q, R, S | protein | 20 | Homo sapiens | P48552 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D), FASTA
>5NTI_1 Nuclear receptor ROR-gamma (chains A, B, C, D)
GPYASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCA
HHLTEAIQYVVEFAKRLSGFMELCQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGK
YGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALVLINAHRPGLQEKRKVEQ
LQYNLELAFHHHLSKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPL
YKELFSTETESPVGLSK
Sequence of entity 2 (P, Q, R, S), FASTA
>5NTI_2 ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN (chains P, Q, R, S)
NSHQKVTLLQLLLGHKNEEN
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| C3S | Cholest-5-en-3-yl hydrogen sulfate | C27 H46 O4 S | 4 |
Primary citation
Structural States of ROR gamma t: X-ray Elucidation of Molecular Mechanisms and Binding Interactions for Natural and Synthetic Compounds. Kallen, J., Izaac, A., Be, C. et al. ChemMedChem (2017) 12:1014-1021. DOI 10.1002/cmdc.201700278 · 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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