This structure does not change between subtypes. It is the same receptor protein regardless of which subtype is selected above — what changes is how much of it that subtype's cells make (the numbers in panel 02), not what it looks like.
This is PDB entry 7BR3, the solved crystal structure of the human GNRHR, published in Nature Communications (Yan et al., 2020). Yellow spheres = elagolix, a small-molecule antagonist bound in the binding pocket.
Caveats, per the PDB file's own DBREF records: (1) elagolix is a small-molecule antagonist, not a peptide agonist such as triptorelin — the molecule LHRH-conjugated nanoparticle constructs use. No structure of GNRHR bound to a peptide agonist has been solved; these are substantially harder to crystallize. (2) This is an engineered fusion construct: PDB residues 1–242 and 257–328 (teal below) are human GNRHR (UniProt P30968). PDB residues 1001–1196 (gray below) are a bacterial (Pyrococcus abyssi) glycogen synthase domain, inserted to stabilize the receptor for crystallization — a standard GPCR crystallography technique, not part of the native receptor.
GNRHR
GlgA fusion (not GNRHR)
Elagolix (ligand)
