8K7R: Human Fc epsilon RI

Human Fc epsilon RI in complex with hIgE Fc (TMD disordered). Determined by electron microscopy at 3.56 Å resolution. Released 4 Dec 2024.

Method: Electron microscopy
Resolution: 3.56 Å
Organism: Homo sapiens
Chains: 3
Atoms: 6,472
Mol. weight: 115.06 kDa
Ligands: NAG
Released: 4 Dec 2024

Explore 8K7R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8K7R contains 27 α-helices and 76 β-strands across 3 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, 18 β-strands

Element	Residues	Length	Sheet
β-strand	32-35	4	1
β-strand	41-42	2	2
β-strand	46-51	6	1
β-strand	64-65	2	3
β-strand	77-81	5	1
α-helix	85-87	3
β-strand	89-91	3	4
β-strand	92-93	2	3
β-strand	104-106	3	4
β-strand	108-109	2	2
β-strand	113-117	5	5
β-strand	128-134	7	5
β-strand	141-147	7	6
β-strand	150-155	6	6
β-strand	161-163	3	5
β-strand	172-174	3	7
β-strand	176-180	5	6
β-strand	183-186	4	6
β-strand	190-192	3	7

Chain E: 13 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	114-117	4	8
β-strand	118-119	2	9
α-helix	120-121	2
β-strand	122	1	10
β-strand	126	1	10
α-helix	127-128	2
β-strand	132-133	2	11
β-strand	134-137	4	8
β-strand	145-151	7	12
β-strand	157-161	5	12
β-strand	178-179	2	11
β-strand	191-197	7	12
β-strand	200-206	7	12
β-strand	207	1	13
α-helix	209-211	3
α-helix	214-216	3
β-strand	218-221	4	14
α-helix	226	1
α-helix	227-231	5
β-strand	236-244	9	14
β-strand	253-257	5	15
β-strand	267-271	5	14
β-strand	278-285	8	14
α-helix	288-293	6
β-strand	296-301	6	15
β-strand	310-315	6	15
α-helix	316-318	3
β-strand	322	1	16
β-strand	325-330	6	17
α-helix	331-334	4
β-strand	341-348	8	17
β-strand	351	1	16
β-strand	356-361	6	18
β-strand	364-365	2	18
α-helix	366-367	2
α-helix	368-370	3
β-strand	371-373	3	17
α-helix	374-376	3
β-strand	377-378	2	17
β-strand	384-392	9	17
α-helix	394-398	5
β-strand	403-408	6	18
β-strand	417-422	6	18

Chain F: 13 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	113-118	6	9
β-strand	121	1	13
β-strand	122	1	19
β-strand	126	1	19
β-strand	131-138	8	9
β-strand	146-151	6	20
β-strand	173-180	8	9
α-helix	182-186	5
β-strand	191-196	6	20
β-strand	203	1	20
β-strand	206	1	20
α-helix	208-210	3
α-helix	214-217	4
β-strand	218-222	5	21
α-helix	223-225	3
α-helix	226	1
α-helix	227-231	5
β-strand	236-242	7	21
β-strand	252-257	6	22
β-strand	267-272	6	21
β-strand	278-285	8	21
α-helix	288-293	6
β-strand	297-302	6	22
α-helix	309	1
β-strand	310-314	5	22
β-strand	322	1	23
β-strand	325-330	6	24
α-helix	331-334	4
β-strand	340-350	11	24
β-strand	351	1	23
β-strand	355-361	7	25
β-strand	364-365	2	25
α-helix	366-367	2
β-strand	371-373	3	24
α-helix	374-376	3
β-strand	377-378	2	24
β-strand	384-393	10	24
α-helix	394-398	5
α-helix	401-402	2
β-strand	403-409	7	25
β-strand	418-422	5	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High affinity immunoglobulin epsilon receptor subunit alpha	A	protein	280	Homo sapiens	P12319 (AlphaFold model)
IgE Fc	E, F	protein	351	Homo sapiens

Sequence of entity 1 (A), FASTA

>8K7R_1 High affinity immunoglobulin epsilon receptor subunit alpha (chains A)
MAPAMESPTLLCVALLFFAPDGVLAVPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVS
STKWFHNGSLSEETNSSLNIVNAKFEDSGEYKCQHQQVNESEPVYLEVFSDWLLLQASAE
VVMEGQPLFLRCHGWRNWDVYKVIYYKDGEALKYWYENHNISITNATVEDSGTYYCTGKV
WQLDYESEPLNITVIKAPREKYWLQFFIPLLVVILFAVDTGLFISTQQQVTFLLKIKRTR
KGFRLLNPHPKPNPKNNENLYFQGDYKDDDDKHHHHHHHH

Sequence of entity 2 (E, F), FASTA

>8K7R_2 IgE Fc (chains E, F)
METGLRWLLLVAVLKGVQCQSVASRDFTPPTVKILQSSCDGGGHFPPTIQLLCLVSGYTP
GTIQITWLEDGQVMDVDLSTASTTQEGELASTQSELTLSQKHWLSDRTYTCQVTYQGHTF
EDSTKKCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVQLTWSRASGKP
VNHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRA
APEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGS
GFFVFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPHHHHHHH

Ligands and cofactors

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

Primary citation

Architecture of the high-affinity immunoglobulin E receptor. Zhang, Z., Yui, M., Ohto, U. et al. Sci Signal (2024) 17:eadn1303-eadn1303. DOI 10.1126/scisignal.adn1303 · 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)
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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