8Z0T: Human ige-fc

Structure of the human ige-fc bound to its high affinity receptor fc(epsilon). Determined by electron microscopy at 3.58 Å resolution. Released 10 Jul 2024.

Method: Electron microscopy
Resolution: 3.58 Å
Organism: Homo sapiens
Chains: 3
Atoms: 6,556
Mol. weight: 111.85 kDa
Ligands: NAG
Released: 10 Jul 2024

Explore 8Z0T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8Z0T contains 29 α-helices and 77 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: 4 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	31-35	5	1
β-strand	40-42	3	2
β-strand	47-52	6	1
β-strand	62-65	4	3
β-strand	70-71	2	3
β-strand	77-80	4	1
α-helix	85-87	3
β-strand	89-91	3	4
β-strand	92-95	4	3
β-strand	100	1	3
α-helix	101-103	3
β-strand	104-106	3	4
β-strand	107-109	3	2
β-strand	113-117	5	5
β-strand	121-122	2	6
β-strand	128-134	7	5
α-helix	135-137	3
β-strand	141-147	7	7
β-strand	150-155	6	7
β-strand	160-163	4	5
β-strand	172-180	9	7
β-strand	183-184	2	7
α-helix	187-189	3
β-strand	190-192	3	7
β-strand	193-194	2	6

Chain D: 13 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	113-117	5	8
β-strand	131-140	10	8
β-strand	146-151	6	9
β-strand	155	1	9
α-helix	163-165	3
β-strand	166-168	3	8
β-strand	171-180	10	8
α-helix	182-186	5
β-strand	190-197	8	9
β-strand	200-207	8	9
β-strand	218-222	5	10
α-helix	223-225	3
α-helix	226	1
α-helix	227-231	5
β-strand	236-244	9	10
β-strand	252-257	6	11
β-strand	267-272	6	10
β-strand	278-285	8	10
α-helix	288-292	5
α-helix	295-296	2
β-strand	297-302	6	11
β-strand	310-314	5	11
α-helix	316-318	3
β-strand	322	1	12
α-helix	323-324	2
β-strand	325-329	5	13
β-strand	340-350	11	13
β-strand	351	1	12
β-strand	356-360	5	14
β-strand	361	1	15
β-strand	364	1	15
α-helix	365-367	3
α-helix	373-376	4
β-strand	377-378	2	13
β-strand	384-393	10	13
α-helix	394-397	4
α-helix	401-402	2
β-strand	403-408	6	14
β-strand	418-422	5	14

Chain E: 12 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	111-112	2
β-strand	113-118	6	16
β-strand	119	1	8
α-helix	127-128	2
β-strand	132-140	9	16
β-strand	146-151	6	17
β-strand	160	1	16
β-strand	168	1	18
β-strand	171	1	18
β-strand	172-174	3	16
β-strand	177-179	3	16
α-helix	185-187	3
β-strand	191-197	7	17
β-strand	200-206	7	17
α-helix	208-211	4
β-strand	219-222	4	19
α-helix	223-225	3
β-strand	236-242	7	19
α-helix	244-246	3
β-strand	252-256	5	20
β-strand	267-268	2	19
β-strand	271-272	2	19
β-strand	278-285	8	19
α-helix	288-293	6
β-strand	297-302	6	20
β-strand	310-314	5	20
β-strand	322	1	21
β-strand	327-329	3	22
α-helix	332-334	3
β-strand	343-348	6	22
β-strand	351	1	21
β-strand	356-361	6	23
β-strand	364-365	2	23
α-helix	366-367	2
β-strand	371-372	2	22
α-helix	373-375	3
β-strand	377-378	2	22
α-helix	379	1
β-strand	384-390	7	22
α-helix	394-398	5
β-strand	403-408	6	23
β-strand	417-422	6	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High affinity immunoglobulin epsilon receptor subunit alpha	A	protein	257	Homo sapiens	P12319 (AlphaFold model)
Isoform 1 of Immunoglobulin heavy constant epsilon	D, E	protein	353	Homo sapiens	P01854 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8Z0T_1 High affinity immunoglobulin epsilon receptor subunit alpha (chains A)
MAPAMESPTLLCVALLFFAPDGVLAVPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVS
STKWFHNGSLSEETNSSLNIVNAKFEDSGEYKCQHQQVNESEPVYLEVFSDWLLLQASAE
VVMEGQPLFLRCHGWRNWDVYKVIYYKDGEALKYWYENHNISITNATVEDSGTYYCTGKV
WQLDYESEPLNITVIKAPREKYWLQFFIPLLVVILFAVDTGLFISTQQQVTFLLKIKRTR
KGFRLLNPHPKPNPKNN

Sequence of entity 2 (D, E), FASTA

>8Z0T_2 Isoform 1 of Immunoglobulin heavy constant epsilon (chains D, E)
MSVPTQVLGLLLLWLTDARCDIVASRDFTPPTVKILQSSCDGGGHFPPTIQLLCLVSGYT
PGTINITWLEDGQVMDVDLSTASTTQEGELASTQSELTLSQKHWLSDRTYTCQVTYQGHT
FEDSTKKCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGK
PVNHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPR
AAPEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKG
SGFFVFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPGKHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	5

Primary citation

Structural insights into the high-affinity IgE receptor Fc epsilon RI complex. Deng, M., Du, S., Hou, H. et al. Nature (2024) 633:952-959. DOI 10.1038/s41586-024-07864-5 · 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)
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

Browse structure collections

About this viewer

MolViewer shows 8Z0T 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.