8YVU: Ige receptor

structure of Ige receptor. Determined by electron microscopy at 3.9 Å resolution. Released 6 Nov 2024.

Method: Electron microscopy
Resolution: 3.9 Å
Organism: Homo sapiens
Chains: 8
Atoms: 4,216
Mol. weight: 62.35 kDa
Ligands: CLR
Released: 6 Nov 2024

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

Secondary structure: helices and β-sheets

8YVU contains 21 α-helices and 0 β-strands across 8 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	207-234	28

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	50-56	7
α-helix	59-82	24
α-helix	96-98	3
α-helix	100-103	4
α-helix	105-120	16
α-helix	126-158	33
α-helix	159-163	5
α-helix	173-204	32

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	26-33	8
α-helix	35-52	18

Chains D and H: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	26-58	33

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	207-233	27

Chain F: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	50-56	7
α-helix	59-82	24
α-helix	100-120	21
α-helix	126-158	33
α-helix	159-163	5
α-helix	173-204	32

Chain G: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	28-52	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High affinity immunoglobulin epsilon receptor subunit alpha	A, E	protein	37	Homo sapiens	P12319 (AlphaFold model)
High affinity immunoglobulin epsilon receptor subunit beta	B, F	protein	160	Homo sapiens	Q01362 (AlphaFold model)
High affinity immunoglobulin epsilon receptor subunit gamma	C, D, G, H	protein	39	Homo sapiens	P30273 (AlphaFold model)

Sequence of entity 1 (A, E), FASTA

>8YVU_1 High affinity immunoglobulin epsilon receptor subunit alpha (chains A, E)
KYWLQFFIPLLVVILFAVDTGLFISTQQQVTFLLKIK

Sequence of entity 2 (B, F), FASTA

>8YVU_2 High affinity immunoglobulin epsilon receptor subunit beta (chains B, F)
TWLTVLKKEQEFLGVTQILTAMICLCFGTVVCSVLDISHIEGDIFSSFKAGYPFWGAIFF
SISGMLSIISERRNATYLVRGSLGANTASSIAGGTGITILIINLKKSLAYIHIHSCQKFF
ETKCFMASFSTEIVVMMLFLTILGLGSAVSLTICGAGEEL

Sequence of entity 3 (C, D, G, H), FASTA

>8YVU_3 High affinity immunoglobulin epsilon receptor subunit gamma (chains C, D, G, H)
PQLCYILDAILFLYGIVLTLLYCRLKIQVRKAAITSYEK

Ligands and cofactors

ID	Name	Formula	Copies
CLR	Cholesterol	C27 H46 O	2

Primary citation

Molecular mechanism of IgE-mediated Fc epsilon RI activation. Chen, M., Su, Q., Shi, Y. Nature (2025) 637:453-460. DOI 10.1038/s41586-024-08229-8 · PubMed

Other PDB entries of the same protein (UniProt P12319 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1F2Q 2.4 Å, Crystal structure of the human high-affinity IgE receptor
1RPQ 3.0 Å, High Affinity IgE Receptor (alpha chain) Complexed with Tight-Binding E131 'zeta'…
8YWA 3.14 Å, The structure of IgE receptor binding to IgE
1J86 3.2 Å, Human high affinity fc receptor fc(epsilon)ri(alpha), monoclinic crystal form 2
1J87 3.2 Å, Human high affinity fc receptor fc(epsilon)ri(alpha), hexagonal crystal form 1
1J88 3.2 Å, Human high affinity fc receptor fc(epsilon)ri(alpha), tetragonal crystal form 1
2Y7Q 3.4 Å, The high-affinity complex between IgE and its receptor fc epsilon ri
1F6A 3.5 Å, Structure of the human ige-fc bound to its high affinity receptor fc(epsilon)ri(alpha)
8K7R 3.56 Å, Human Fc epsilon RI in complex with hIgE Fc (TMD disordered)
8Z0T 3.58 Å, Structure of the human ige-fc bound to its high affinity receptor fc(epsilon)
8C1B 3.8 Å, Focused map for structure of IgE bound to the ectodomain of FceRIa
1J89 4.1 Å, Human high affinity fc receptor fc(epsilon)ri(alpha), tetragonal crystal form 2

Browse structure collections

About this viewer

MolViewer shows 8YVU 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.