1F2Q: Human high-affinity IgE receptor

Crystal structure of the human high-affinity IgE receptor. Determined by X-ray diffraction at 2.4 Å resolution. Released 8 Jun 2000.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,536
Mol. weight: 21.86 kDa
Ligands: NAG
Released: 8 Jun 2000

Explore 1F2Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F2Q contains 5 α-helices and 19 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 A: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	1
β-strand	15-17	3	2
β-strand	22-25	4	1
β-strand	38-41	4	3
β-strand	44-45	2	3
β-strand	52-55	4	1
α-helix	60-62	3
β-strand	64-69	6	3
α-helix	75-78	4
β-strand	79-81	3	3
β-strand	82-84	3	2
β-strand	88-92	5	4
β-strand	96-98	3	5
β-strand	103-109	7	4
α-helix	110-112	3
β-strand	115-122	8	6
β-strand	125-126	2	6
β-strand	135-138	4	4
α-helix	143-145	3
β-strand	147-155	9	6
β-strand	158-161	4	6
α-helix	162-164	3
β-strand	165-167	3	6
β-strand	168-170	3	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High affinity immunoglobulin epsilon receptor alpha-subunit	A	protein	176	Homo sapiens	P12319 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1F2Q_1 HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT (chains A)
VPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKF
EDSGEYKCQHQQVNESEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIY
YKDGEALKYWYENHNISITNATVEDSGTYYCTGKVWQLDYESEPLNITVIKAPREK

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

Crystal structure of the human high-affinity IgE receptor. Garman, S.C., Kinet, J.P., Jardetzky, T.S. Cell (1998) 95:951-961. DOI 10.1016/S0092-8674(00)81719-5 · PubMed

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

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
8YVU 3.9 Å, structure of Ige receptor
1J89 4.1 Å, Human high affinity fc receptor fc(epsilon)ri(alpha), tetragonal crystal form 2

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