Structure of beta2 adrenergic receptor fused to a Gs peptide. Determined by X-ray diffraction at 3.7 Å resolution. Released 5 Jun 2019.
Explore 6E67 in 3D Show helices and sheets RCSB PDB PDBe
6E67 contains 56 α-helices and 8 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 | 30-59 | 30 | |
| α-helix | 67-81 | 15 | |
| α-helix | 82-86 | 5 | |
| α-helix | 87-96 | 10 | |
| α-helix | 103-136 | 34 | |
| α-helix | 138-144 | 7 | |
| α-helix | 147-170 | 24 | |
| α-helix | 179-186 | 8 | |
| α-helix | 197-204 | 8 | |
| α-helix | 205-209 | 5 | |
| α-helix | 210-225 | 16 | |
| α-helix | 226-228 | 3 | |
| α-helix | 229-1007 | 10 | |
| α-helix | 1008-1012 | 5 | |
| β-strand | 1014-1019 | 6 | 1 |
| β-strand | 1025-1028 | 4 | 1 |
| β-strand | 1031-1034 | 4 | 1 |
| α-helix | 1039-1050 | 12 | |
| α-helix | 1060-1080 | 21 | |
| α-helix | 1085-1090 | 6 | |
| α-helix | 1093-1111 | 19 | |
| α-helix | 1115-1122 | 8 | |
| α-helix | 1126-1134 | 9 | |
| α-helix | 1137-1141 | 5 | |
| α-helix | 1143-1155 | 13 | |
| α-helix | 2381-2393 | 13 | |
| α-helix | 268-298 | 31 | |
| α-helix | 305-321 | 17 | |
| α-helix | 322-324 | 3 | |
| α-helix | 330-339 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 20-23 | 4 | |
| α-helix | 30-59 | 30 | |
| α-helix | 62-64 | 3 | |
| α-helix | 67-81 | 15 | |
| α-helix | 82-86 | 5 | |
| α-helix | 87-96 | 10 | |
| α-helix | 102-136 | 35 | |
| α-helix | 138-144 | 7 | |
| α-helix | 147-163 | 17 | |
| α-helix | 167-170 | 4 | |
| β-strand | 175 | 1 | 2 |
| α-helix | 179-186 | 8 | |
| β-strand | 195 | 1 | 2 |
| α-helix | 197-204 | 8 | |
| α-helix | 205-209 | 5 | |
| α-helix | 210-225 | 16 | |
| α-helix | 229-1010 | 13 | |
| β-strand | 1014-1019 | 6 | 3 |
| β-strand | 1025-1028 | 4 | 3 |
| β-strand | 1031-1032 | 2 | 3 |
| α-helix | 1039-1050 | 12 | |
| α-helix | 1060-1080 | 21 | |
| α-helix | 1084-1090 | 7 | |
| α-helix | 1093-1103 | 11 | |
| α-helix | 1108-1112 | 5 | |
| α-helix | 1115-1122 | 8 | |
| α-helix | 1126-1135 | 10 | |
| α-helix | 1137-1141 | 5 | |
| α-helix | 1143-1155 | 13 | |
| α-helix | 2381-2393 | 13 | |
| α-helix | 268-298 | 31 | |
| α-helix | 305-321 | 17 | |
| α-helix | 322-324 | 3 | |
| α-helix | 330-339 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2 adrenergic receptor,Endolysin,Guanine nucleotide-binding protein G(s) subunit alpha… | A, B | protein | 531 | Homo sapiens, Enterobacteria phage RB59 | A0A097J809, P07550 (AlphaFold model), P63092 (AlphaFold model) |
>6E67_1 Beta-2 adrenergic receptor,Endolysin,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,Beta-2 adrenergic receptor chimera (chains A, B) MKTIIALSYIFCLVFADYKDDDDAMGQPGNGSAFLLAPNRSHAPDHDVTQQRDEVWVVGM GIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILT KTWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILM VWIVSGLTSFLPIQMHWYRATHQEAINCYAEETCCDFFTNQAYAIASSIVSFYVPLVIMV FVYSRVFQECKRQLQKNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSE LDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQ MGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYDIIQ RMHLRQYELCGTGEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWI GYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| P0G | 8-[(1R)-2-{[1,1-dimethyl-2-(2-methylphenyl)ethyl]amino}-1-hydroxyethyl]-5-hydro… | C21 H26 N2 O4 | 2 |
Structural Insights into the Process of GPCR-G Protein Complex Formation. Liu, X., Xu, X., Hilger, D. et al. Cell (2019) 177:1243-1251.e12. DOI 10.1016/j.cell.2019.04.021 · PubMed
Other PDB entries of the same protein (UniProt A0A097J809), best resolution first:
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