Crystal structure of the protein 1. Determined by X-ray diffraction at 2.79 Å resolution. Released 7 Oct 2020.
Explore 7BR3 in 3D Show helices and sheets RCSB PDB PDBe
7BR3 contains 23 α-helices and 12 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 28 | 1 | 1 |
| α-helix | 33-62 | 30 | |
| α-helix | 75-94 | 20 | |
| α-helix | 95-101 | 7 | |
| β-strand | 104 | 1 | 1 |
| α-helix | 111-141 | 31 | |
| α-helix | 155-170 | 16 | |
| α-helix | 173-177 | 5 | |
| β-strand | 179-181 | 3 | 2 |
| β-strand | 195-197 | 3 | 2 |
| α-helix | 205-216 | 12 | |
| α-helix | 217-221 | 5 | |
| α-helix | 222-241 | 20 | |
| α-helix | 1009-1011 | 3 | |
| α-helix | 1016-1027 | 12 | |
| β-strand | 1033-1038 | 6 | 3 |
| α-helix | 1048-1059 | 12 | |
| α-helix | 1064-1066 | 3 | |
| β-strand | 1067-1072 | 6 | 3 |
| α-helix | 1077-1089 | 13 | |
| β-strand | 1093-1096 | 4 | 3 |
| α-helix | 1102-1109 | 8 | |
| β-strand | 1114-1117 | 4 | 3 |
| β-strand | 1122 | 1 | 4 |
| α-helix | 1127-1133 | 7 | |
| α-helix | 1136 | 1 | |
| β-strand | 1137-1141 | 5 | 3 |
| β-strand | 1144 | 1 | 4 |
| α-helix | 1145-1149 | 5 | |
| β-strand | 1156-1158 | 3 | 3 |
| α-helix | 1163-1175 | 13 | |
| α-helix | 1183-1196 | 14 | |
| α-helix | 260-292 | 33 | |
| α-helix | 294-299 | 6 | |
| α-helix | 302-325 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gonadotropin-releasing hormone receptor,GlgA glycogen synthase,Gonadotropin-releasing hormone… | A | protein | 528 | Homo sapiens, Pyrococcus abyssi (strain GE5 / Orsay) | P30968 (AlphaFold model), Q9V2J8 (AlphaFold model) |
>7BR3_1 Gonadotropin-releasing hormone receptor,GlgA glycogen synthase,Gonadotropin-releasing hormone receptor (chains A) DYKDDDDAMANSASPEQNQNHCSAINNSIPLMQGNLPTLTLSGKIRVTVTFFLFLLSATF NASFLLKLQKWTQKKEKGKKLSRMKLLLKHLTLANLLETLIVMPLDGMWNITVQWYAGEL LCKVLSYLKLFSMYAKAFMMVVISLDRSLAITRPLALKSNSKVGQSMVGLAWILSSVFAG PQLYIFRMIHLADSSGQTKVFSQCVTHCSFSQWWHQAFYNFFTFSCLFIIPLFIMLICNA KIIFTLTRVLGIDCSFWNESYLTGSRDERKKSLLSKFGMDEGVTFMFIGRFDRGQKGVDV LLKAIEILSSKKEFQEMRFIIIGKGDPELEGWARSLEEKHGNVKVITEMLSREFVRELYG SVDFVIIPSYFEPFGLVALEAMCLGAIPIASAVGGLRDIITNETGILVKAGDPGELANAI LKALELSRSDLSKFRENCKKRAMSFSNIPRARLKTLKMTVAFATSFTVCWTPYYVLGIWY WFDPEMLNRLSDPVNHFFFLFAFLNPCFDPLIYGYFSLHHHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| 1QW | (2R)-2,3-dihydroxypropyl dodecanoate | C15 H30 O4 | 1 |
| OLC | (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate | C21 H40 O4 | 2 |
| F5O | 4-[[(1R)-2-[5-(2-fluoranyl-3-methoxy-phenyl)-3-[[2-fluoranyl-6-(trifluoromethyl… | C32 H30 F5 N3 O5 | 1 |
Water and common crystallization additives (PEG, FMT) are not listed.
Structure of the human gonadotropin-releasing hormone receptor GnRH1R reveals an unusual ligand binding mode. Yan, W., Cheng, L., Wang, W. et al. Nat Commun (2020) 11:5287-5287. DOI 10.1038/s41467-020-19109-w · PubMed
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