9LRS: MRGPRX4 with PSB-18061
The structure of MRGPRX4 with PSB-18061. Determined by electron microscopy at 2.83 Å resolution. Released 4 Feb 2026.
- Method
- Electron microscopy
- Resolution
- 2.83 Å
- Organisms
- Escherichia coli, Homo sapiens, Mus musculus
- Chains
- 5
- Atoms
- 8,137
- Mol. weight
- 157.94 kDa
- Ligands
- A1L7J
- Released
- 4 Feb 2026
Explore 9LRS in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9LRS contains 35 α-helices and 57 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 B: 8 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-31 | 25 | |
| β-strand | 33-39 | 7 | 1 |
| α-helix | 46-48 | 3 | |
| β-strand | 69-76 | 8 | 1 |
| β-strand | 79-86 | 8 | 1 |
| β-strand | 105-111 | 7 | 1 |
| α-helix | 118-129 | 12 | |
| α-helix | 132-134 | 3 | |
| β-strand | 138-144 | 7 | 1 |
| α-helix | 146-155 | 10 | |
| α-helix | 160-163 | 4 | |
| α-helix | 184-203 | 20 | |
| β-strand | 211-215 | 5 | 1 |
| α-helix | 223-242 | 20 | |
Chain C: 5 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-24 | 21 | |
| α-helix | 30-33 | 4 | |
| α-helix | 34-36 | 3 | |
| β-strand | 47-51 | 5 | 2 |
| β-strand | 58-63 | 6 | 3 |
| β-strand | 69-74 | 6 | 3 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 88-94 | 7 | 3 |
| β-strand | 100-105 | 6 | 4 |
| β-strand | 111-116 | 6 | 4 |
| β-strand | 120-125 | 6 | 4 |
| α-helix | 129-131 | 3 | |
| β-strand | 134-140 | 7 | 4 |
| β-strand | 146-153 | 8 | 5 |
| β-strand | 156-161 | 6 | 5 |
| β-strand | 166-170 | 5 | 5 |
| β-strand | 175-180 | 6 | 5 |
| β-strand | 187-192 | 6 | 6 |
| β-strand | 198-203 | 6 | 6 |
| β-strand | 208-212 | 5 | 6 |
| β-strand | 218-222 | 5 | 6 |
| β-strand | 229-234 | 6 | 7 |
| β-strand | 240-245 | 6 | 7 |
| β-strand | 250-254 | 5 | 7 |
| β-strand | 259-264 | 6 | 7 |
| α-helix | 272 | 1 | |
| β-strand | 273-278 | 6 | 8 |
| β-strand | 284-289 | 6 | 8 |
| β-strand | 294-298 | 5 | 8 |
| β-strand | 304-308 | 5 | 8 |
| β-strand | 315-320 | 6 | 2 |
| β-strand | 327-331 | 5 | 2 |
| β-strand | 336-339 | 4 | 2 |
Chain D: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-23 | 11 | |
| α-helix | 30-43 | 14 | |
| α-helix | 44-46 | 3 | |
| α-helix | 53-55 | 3 | |
Chain E: 4 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 9 |
| β-strand | 11-12 | 2 | 10 |
| β-strand | 17-25 | 9 | 9 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 11 |
| β-strand | 45-51 | 7 | 11 |
| β-strand | 58-60 | 3 | 11 |
| β-strand | 65 | 1 | 9 |
| β-strand | 68-73 | 6 | 9 |
| β-strand | 78-84 | 7 | 9 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 11 |
| β-strand | 111-117 | 7 | 11 |
| β-strand | 118-119 | 2 | 10 |
| β-strand | 134 | 1 | 12 |
| β-strand | 143-148 | 6 | 13 |
| β-strand | 154 | 1 | 14 |
| β-strand | 160 | 1 | 14 |
| β-strand | 162-167 | 6 | 12 |
| β-strand | 174-178 | 5 | 12 |
| β-strand | 182-183 | 2 | 12 |
| α-helix | 184 | 1 | |
| β-strand | 191-196 | 6 | 13 |
| β-strand | 199-204 | 6 | 13 |
| β-strand | 214-219 | 6 | 12 |
| α-helix | 225 | 1 | |
| β-strand | 232 | 1 | 12 |
Chain R: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-54 | 28 | |
| α-helix | 62-86 | 25 | |
| α-helix | 92-125 | 34 | |
| α-helix | 127-132 | 6 | |
| α-helix | 138-154 | 17 | |
| α-helix | 179-203 | 25 | |
| α-helix | 211-223 | 13 | |
| α-helix | 224-229 | 6 | |
| α-helix | 230-236 | 7 | |
| α-helix | 246-249 | 4 | |
| α-helix | 250-254 | 5 | |
| α-helix | 255-269 | 15 | |
| α-helix | 270-274 | 5 | |
| α-helix | 275-279 | 5 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Soluble cytochrome b562,Mas-related G-protein coupled receptor member X4 | R | protein | 472 | Escherichia coli, Homo sapiens | P0ABE7 (AlphaFold model), Q96LA9 (AlphaFold model) |
| Gs-mini-Gq chimera | B | protein | 246 | Homo sapiens | |
| Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | C | protein | 358 | Homo sapiens | P62873 (AlphaFold model) |
| Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | D | protein | 71 | Homo sapiens | P59768 (AlphaFold model) |
| scFv16 | E | protein | 267 | Mus musculus | |
Sequence of entity 1 (R), FASTA
>9LRS_1 Soluble cytochrome b562,Mas-related G-protein coupled receptor member X4 (chains R)
DYKDDDDAKLQTMHHHHHHHHHHENLYFQGGTTMADLEDNWETLNDNLKVIEKADNAAQV
KDALTKMRAAALDAQKATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKE
AQAAAEQLKTTRNAYIQKYLGSTLEVLFQGPDPTVPVFGTKLTPINGREETPCYNQTLSF
TVLTCIISLVGLTGNAVVLWLLGYRMRRNAVSIYILNLAAADFLFLSFQIIRSPLRLINI
SHLIRKILVSVMTFPYFTGLSMLSAISTERCLSVLWPIWYRCRRPTHLSAVVCVLLWGLS
LLFSMLEWRFCDFLFSGADSSWCETSDFIPVAWLIFLCVVLCVSSLVLLVRILCGSRKMP
LTRLYVTILLTVLVFLLCGLPFGILGALIYRMHLNLEVLYCHVYLVCMSLSSLNSSANPI
IYFFVGSFRQRQNRQNLKLVLQRALQDKPEVDKGEGQLPEESLELSGSRLGP
Sequence of entity 2 (B), FASTA
>9LRS_2 Gs-mini-Gq chimera (chains B)
MGSTVSAEDKAAAERSKMIDKNLREDGEKARRTLRLLLLGADNSGKSTIVKQMRILHGGS
GGSGGTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVDSSDYNRLQE
ALNDFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEP
GEDPRVTRAKYFIRKEFVDISTASGDGRHICYPHFTCAVDTENARRIFNDCKDIILQMNL
REYNLV
Sequence of entity 3 (C), FASTA
>9LRS_3 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (chains C)
MHHHHHHLEVLFQGPGSSGSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGR
IQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMT
CAYAPSGNYVACGGLDNICSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSG
DTTCALWDIETGQQTTTFTGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTF
TGHESDINAICFFPNGNAFATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSG
RLLLAGYDDFNCNVWDALKADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Sequence of entity 4 (D), FASTA
>9LRS_4 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 (chains D)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Sequence of entity 5 (E), FASTA
>9LRS_5 scFv16 (chains E)
DVQLVESGGGLVQPGGSRKLSCSASGFAFSSFGMHWVRQAPEKGLEWVAYISSGSGTIYY
ADTVKGRFTISRDDPKNTLFLQMTSLRSEDTAMYYCVRSIYYYGSSPFDFWGQGTTLTVS
SGGGGSGGGGSGGGGSDIVMTQATSSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQR
PGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLTISRLEAEDVGVYYCMQHLEYPLTFG
AGTKLELKAAALEVLFQGPHHHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| A1L7J | 4-[7-methyl-2,6-bis(oxidanylidene)-1-prop-2-ynyl-8-[2-[3-(trifluoromethyl)pheny… | C22 H24 F3 N4 O5 P | 1 |
Primary citation
The structure of MRGPRX4 with PSB-18061. Cao, C., Roth, B.L. To be published.
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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