Crystal structure of the Orexin-1 receptor in complex with Compound 16. Determined by X-ray diffraction at 2.3 Å resolution. Released 1 Jan 2020.
Explore 6TQ4 in 3D Show helices and sheets RCSB PDB PDBe
6TQ4 contains 31 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-35 | 8 | |
| α-helix | 36-40 | 5 | |
| α-helix | 41-73 | 33 | |
| α-helix | 75-77 | 3 | |
| α-helix | 80-94 | 15 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-109 | 10 | |
| α-helix | 115-148 | 34 | |
| α-helix | 158-175 | 18 | |
| α-helix | 177-182 | 6 | |
| β-strand | 183-187 | 5 | 1 |
| β-strand | 200-204 | 5 | 1 |
| α-helix | 210-220 | 11 | |
| α-helix | 221-225 | 5 | |
| α-helix | 226-242 | 17 | |
| α-helix | 288-322 | 35 | |
| α-helix | 333-361 | 29 | |
| α-helix | 363-374 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 46-73 | 28 | |
| α-helix | 75-77 | 3 | |
| α-helix | 80-94 | 15 | |
| α-helix | 95-99 | 5 | |
| α-helix | 100-109 | 10 | |
| α-helix | 115-148 | 34 | |
| α-helix | 158-175 | 18 | |
| α-helix | 177-182 | 6 | |
| β-strand | 183-187 | 5 | 2 |
| α-helix | 192-194 | 3 | |
| β-strand | 200-204 | 5 | 2 |
| α-helix | 210-220 | 11 | |
| α-helix | 221-225 | 5 | |
| α-helix | 226-243 | 18 | |
| α-helix | 252-322 | 71 | |
| α-helix | 334-361 | 28 | |
| α-helix | 363-375 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Orexin receptor type 1 | A, B | protein | 368 | Homo sapiens | O43613 (AlphaFold model) |
>6TQ4_1 Orexin receptor type 1 (chains A, B) AASEDEFLRYLWRDYLYPKQYAWVLIAAYVAVFVVALVGNTLVCLAVWRNHHMRTVTNYF LVNLSLADVLATAICLPASLLVDITESWLFGHALCKVIPYLQAVSVSVAVLTLSFIALDR WYAICHPLLFKSTARRALGSILGIWAVSLAIMVPQAAVMECSSVLPELAARTRAFSVCDE RWADDLAPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSDQ LGDLEQGLSGEPQPRARAFLAEVKQMRARRKTAKMLMVVVLVFALCYLPISVLNVLKRVF GMFRQASDREAVYAAFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSWWLPGLAAAH HHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NV8 | 2-[1-(phenylsulfonyl)-1,8-diazaspiro[4.5]decan-8-yl]-1,3-benzoxazole | C21 H23 N3 O3 S | 2 |
| PGW | (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexade… | C40 H77 O10 P | 2 |
| SOG | octyl 1-thio-beta-D-glucopyranoside | C14 H28 O5 S | 13 |
Water and common crystallization additives (SO4, NA) are not listed.
Comparison of Orexin 1 and Orexin 2 Ligand Binding Modes Using X-ray Crystallography and Computational Analysis. Rappas, M., Ali, A.A.E., Bennett, K.A. et al. J Med Chem (2020) 63:1528-1543. DOI 10.1021/acs.jmedchem.9b01787 · PubMed
Other PDB entries of the same protein (UniProt O43613 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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