8KEX: Gq coupled MRGPRX4 with agonist DCA-3P, local

CryoEM structure of Gq coupled MRGPRX4 with agonist DCA-3P, local. Determined by electron microscopy at 3.2 Å resolution. Released 6 Nov 2024.

Method: Electron microscopy
Resolution: 3.2 Å
Organisms: Escherichia coli, Homo sapiens, Aequorea victoria
Chains: 1
Atoms: 1,988
Mol. weight: 80.27 kDa
Ligands: JW0
Released: 6 Nov 2024

Explore 8KEX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8KEX contains 13 α-helices and 0 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.

Chain E: 13 helices, 0 β-strands

Element	Residues	Length
α-helix	28-54	27
α-helix	62-82	21
α-helix	83-85	3
α-helix	94-125	32
α-helix	127-128	2
α-helix	129-133	5
α-helix	138-151	14
α-helix	179-203	25
α-helix	213-226	14
α-helix	230-241	12
α-helix	253-269	17
α-helix	270-274	5
α-helix	275-278	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Soluble cytochrome b562,Mas-related G-protein coupled receptor member X4,Green fluorescent protein	E	protein	710	Escherichia coli, Homo sapiens, Aequorea victoria	P0ABE7 (AlphaFold model), P42212 (AlphaFold model), Q96LA9 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>8KEX_1 Soluble cytochrome b562,Mas-related G-protein coupled receptor member X4,Green fluorescent protein (chains E)
DYKDDDDKEFADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLED
KSPDSPEMKDFRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQKYLMDPT
VPVFGTKLTPINGREETPCYNQTLSFTVLTCIISLVGLTGNAVVLWLLGYRMRRNAVSIY
ILNLAAADFLFLSFQIIRLPLRLINISHLIRKILVSVMTFPYFTGLSMLSAISTERCLSV
LWPIWYRCRRPTHLSAVVCVLLWGLSLLFSMLEWRFCDFLFSGADSSWCETSDFIPVAWL
IFLCVVLCVSSLVLLVRILCGSRKMPLTRLYVTILLTVLVFLLCGLPFGILGALIYRMHL
NLEVLYCHVYLVCMSLSSLNSSANPIIYFFVGSFRQRQNRQNLKLVLQRALQDKPEVDKG
EGQLPEESLELSGSRLGPLELEVLFQGPSKGEELFTGVVPILVELDGDVNGHKFSVRGEG
EGDATNGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYV
QERTISFKDDGTYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNFNSHNVYIT
ADKQKNGIKANFKIRHNVEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSVLSKDPNE
KRDHMVLLEFVTAAGITHGMDEWSHPQFEKGGGSGGGSGGSAWSHPQFEK

Ligands and cofactors

ID	Name	Formula	Copies
JW0	(4~{R})-4-[(3~{R},5~{R},8~{R},9~{S},10~{S},12~{S},13~{R},14~{S},17~{R})-10,13-d…	C24 H41 O7 P	1

Primary citation

Structure-guided discovery of bile acid derivatives for treating liver diseases without causing itch. Yang, J., Zhao, T., Fan, J. et al. Cell (2024) 187:7164-7182.e18. DOI 10.1016/j.cell.2024.10.001 · 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

About this viewer

MolViewer shows 8KEX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.