7JVR: Bromocriptine-bound dopamine receptor 2
Cryo-EM structure of Bromocriptine-bound dopamine receptor 2 in complex with Gi protein. Determined by electron microscopy at 2.8 Å resolution. Released 24 Feb 2021.
- Method
- Electron microscopy
- Resolution
- 2.8 Å
- Organisms
- Escherichia coli, Homo sapiens, synthetic construct
- Chains
- 5
- Atoms
- 8,872
- Mol. weight
- 183.12 kDa
- Ligands
- 08Y
- Released
- 24 Feb 2021
Explore 7JVR in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7JVR contains 33 α-helices and 65 β-strands across 5 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: 11 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-32 | 26 | |
| β-strand | 34-39 | 6 | 1 |
| α-helix | 46-54 | 9 | |
| β-strand | 185-190 | 6 | 1 |
| β-strand | 195-200 | 6 | 1 |
| α-helix | 208-210 | 3 | |
| α-helix | 212-216 | 5 | |
| β-strand | 220-225 | 6 | 1 |
| α-helix | 227-229 | 3 | |
| β-strand | 233 | 1 | 2 |
| α-helix | 234 | 1 | |
| β-strand | 241 | 1 | 2 |
| α-helix | 242-254 | 13 | |
| β-strand | 263-268 | 6 | 1 |
| α-helix | 271-280 | 10 | |
| α-helix | 283-285 | 3 | |
| α-helix | 296-310 | 15 | |
| β-strand | 319-323 | 5 | 1 |
| α-helix | 328-351 | 24 | |
Chain B: 2 helices, 32 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-24 | 21 | |
| α-helix | 38-39 | 2 | |
| β-strand | 45-52 | 8 | 3 |
| β-strand | 58-63 | 6 | 4 |
| β-strand | 69-74 | 6 | 4 |
| β-strand | 78-83 | 6 | 4 |
| β-strand | 91-94 | 4 | 4 |
| β-strand | 100-105 | 6 | 5 |
| β-strand | 111-116 | 6 | 5 |
| β-strand | 121-125 | 5 | 5 |
| β-strand | 134-139 | 6 | 5 |
| β-strand | 146-151 | 6 | 6 |
| β-strand | 156-161 | 6 | 6 |
| β-strand | 166-170 | 5 | 6 |
| β-strand | 175-180 | 6 | 6 |
| β-strand | 187 | 1 | 7 |
| β-strand | 191-192 | 2 | 8 |
| β-strand | 198-202 | 5 | 8 |
| β-strand | 203 | 1 | 7 |
| β-strand | 207-212 | 6 | 8 |
| β-strand | 218-223 | 6 | 8 |
| β-strand | 229 | 1 | 9 |
| β-strand | 233-234 | 2 | 10 |
| β-strand | 240-244 | 5 | 10 |
| β-strand | 245 | 1 | 9 |
| β-strand | 250-254 | 5 | 10 |
| β-strand | 259-264 | 6 | 10 |
| β-strand | 273-278 | 6 | 11 |
| β-strand | 284-289 | 6 | 11 |
| β-strand | 294-298 | 5 | 11 |
| β-strand | 304-308 | 5 | 11 |
| β-strand | 315-320 | 6 | 3 |
| β-strand | 327-331 | 5 | 3 |
| β-strand | 335-341 | 7 | 3 |
Chain C: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-23 | 17 | |
| α-helix | 30-43 | 14 | |
| α-helix | 53-55 | 3 | |
Chain E: 1 helix, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 12 |
| β-strand | 12 | 1 | 13 |
| β-strand | 18-25 | 8 | 12 |
| β-strand | 33-39 | 7 | 14 |
| β-strand | 45-51 | 7 | 14 |
| β-strand | 58-60 | 3 | 14 |
| β-strand | 68-73 | 6 | 12 |
| β-strand | 78-83 | 6 | 12 |
| β-strand | 92-99 | 8 | 14 |
| β-strand | 110-111 | 2 | 14 |
| β-strand | 115-117 | 3 | 14 |
| β-strand | 119 | 1 | 13 |
| β-strand | 140-141 | 2 | 15 |
| β-strand | 146-148 | 3 | 16 |
| β-strand | 155-161 | 7 | 15 |
| β-strand | 166 | 1 | 17 |
| β-strand | 172 | 1 | 17 |
| β-strand | 174-179 | 6 | 16 |
| β-strand | 185-190 | 6 | 16 |
| β-strand | 194-195 | 2 | 16 |
| β-strand | 203-206 | 4 | 15 |
| β-strand | 211-216 | 6 | 15 |
| β-strand | 226-231 | 6 | 16 |
| α-helix | 237 | 1 | |
| β-strand | 238 | 1 | 14 |
| β-strand | 243-246 | 4 | 16 |
Chain R: 16 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 35-61 | 27 | |
| α-helix | 68-82 | 15 | |
| α-helix | 83-87 | 5 | |
| α-helix | 88-97 | 10 | |
| α-helix | 104-137 | 34 | |
| α-helix | 139-143 | 5 | |
| α-helix | 145-169 | 25 | |
| α-helix | 170-174 | 5 | |
| α-helix | 187-194 | 8 | |
| α-helix | 195-199 | 5 | |
| α-helix | 200-224 | 25 | |
| α-helix | 366-385 | 20 | |
| α-helix | 387-399 | 13 | |
| α-helix | 405-423 | 19 | |
| α-helix | 424-428 | 5 | |
| α-helix | 431-440 | 10 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Soluble cytochrome b562,D(2) dopamine receptor | R | protein | 588 | Escherichia coli, Homo sapiens | P0ABE7 (AlphaFold model), P14416 (AlphaFold model) |
| Guanine nucleotide-binding protein G(i) subunit alpha-1 | A | protein | 354 | Homo sapiens | P63096 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | B | protein | 348 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | C | protein | 71 | Homo sapiens | P59768 |
| Antibody fragment ScFv16 | E | protein | 269 | synthetic construct | |
Sequence of entity 1 (R), FASTA
>7JVR_1 Soluble cytochrome b562,D(2) dopamine receptor (chains R)
DYKDDDDAKLQTMHHHHHHHHHHHHHHHADLEDNWETLNDNLKVIEKADNAAQVKDALTK
MRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAE
QLKTTRNAYIQKYLASENLYFQGGTMDPLNLSWYDDDLERQNWSRPFNGSDGKADRPHYN
YYATLLTLLIAVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLE
VVGEWKFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVM
ISIVWVLSFTISCPLLFGLNNADQNECIIANPAFVVYSSIVSFYVPFIVTLLVYIKIYIV
LRRRRKRVNTKRSSRAFRAHLRAPLKGNCTHPEDMKLCTVIMKSNGSFPVNRRRVEAARR
AQELEMEMLSSTSPPERTRYSPIPPSHHQLTLPDPSHHGLHSTPDSPAKPEKNGHAKDHP
KIAKIFEIQTMPNGKTRTSLKTMSRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHIL
NIHCDCNIPPVLYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFLKILHC
Sequence of entity 2 (A), FASTA
>7JVR_2 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains A)
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKNTIVKQMKIIHEAG
YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT
AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK
TTGIVETHFTFKDLHFKMFDVGAQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM
NRMHASMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAA
AYIQCQFEDLNKRKDTKEIYTHFTCSTDTKNVQFVFDAVTDVIIKNNLKDCGLF
Sequence of entity 3 (B), FASTA
>7JVR_3 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains B)
MGSLLQSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHL
AKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACG
GLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQ
QTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFF
PNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCN
VWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWNGSS
Sequence of entity 4 (C), FASTA
>7JVR_4 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains C)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Sequence of entity 5 (E), FASTA
>7JVR_5 Antibody fragment ScFv16 (chains E)
DVQLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYY
ADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVS
SGGGGSGGGGSGGGGSDIVMTQATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQR
PGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFG
AGTKLELKGSLEVLFQGPAAAHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 08Y | bromoergocryptine | C32 H40 Br N5 O5 | 1 |
Primary citation
Structural insights into the human D1 and D2 dopamine receptor signaling complexes. Zhuang, Y., Xu, P., Mao, C. et al. Cell (2021) 184:931-942.e18. DOI 10.1016/j.cell.2021.01.027 · PubMed
Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6DYF 1.1 Å, Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y
- 5YO6 1.2 Å, Crystal Structure of B562RIL with engineered disulfide bond T9C-A36C
- 4JEA 1.22 Å, Crystal structure of an engineered Zn-RIDC1 construct with four interfacial disulfide…
- 7LSJ 1.26 Å, Cu-bound crystal structure of the engineered cyt cb562 variant, DiCyt2 - H63A,…
- 7MK4 1.27 Å, Co-bound crystal structure of the engineered cyt cb562 variant, DiCyt2
- 6DYC 1.33 Å, Co(II)-bound structure of the engineered cyt cb562 variant, CH3
- 5YO4 1.37 Å, Crystal Structure of B562RIL with engineered disulfide bond K27C-A79C
- 256B 1.4 Å, Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the…
- 6OT4 1.4 Å, Bimetallic dodecameric cage design 2 (BMC2) from cytochrome cb562
- 7LRV 1.4 Å, Ni-bound crystal structure of the engineered cyt cb562 variant, DiCyt2, crystallized in…
- 9PQ4 1.48 Å, Bi-bound structure of the H77C variant of TriCyt2
- 6DYG 1.49 Å, Fe(II)-bound structure of the engineered cyt cb562 variant, CH3Y
Browse structure collections
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