1F6A: Human ige-fc

Structure of the human ige-fc bound to its high affinity receptor fc(epsilon)ri(alpha). Determined by X-ray diffraction at 3.5 Å resolution. Released 20 Jul 2000.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,251
Mol. weight: 77.39 kDa
Ligands: CPS
Released: 20 Jul 2000

Explore 1F6A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1F6A contains 19 α-helices and 61 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: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	3-6	4
β-strand	7-10	4	1
β-strand	15-17	3	2
β-strand	22-26	5	1
β-strand	38-41	4	3
β-strand	44-45	2	3
α-helix	46	1
β-strand	52-55	4	1
α-helix	60-62	3
β-strand	64-69	6	3
β-strand	79-81	3	3
β-strand	82-84	3	2
β-strand	88-92	5	4
β-strand	96-97	2	5
β-strand	103-109	7	4
α-helix	110-112	3
β-strand	116-122	7	6
β-strand	125-130	6	6
β-strand	135-138	4	4
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	168-169	2	5

Chain B: 7 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	333-335	3
β-strand	338-341	4	7
α-helix	342-344	3
α-helix	345-349	5
β-strand	355-363	9	7
β-strand	373-376	4	8
β-strand	388-391	4	7
β-strand	397-404	8	7
α-helix	407-411	5
β-strand	415-420	6	8
β-strand	429-434	6	8
β-strand	441	1	9
β-strand	444-449	6	10
α-helix	450-452	3
β-strand	453	1	11
β-strand	456	1	11
β-strand	459-469	11	10
β-strand	470	1	9
β-strand	475-476	2	12
β-strand	479	1	13
α-helix	487-489	3
β-strand	491-492	2	10
β-strand	496-497	2	10
β-strand	503-512	10	10
α-helix	513-518	6
β-strand	522-523	2	13
β-strand	526-527	2	12
β-strand	536-537	2	12
β-strand	540-541	2	13

Chain D: 7 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	337-341	5	14
α-helix	342-344	3
α-helix	345-349	5
β-strand	355-363	9	14
β-strand	372-376	5	15
β-strand	388-391	4	14
β-strand	397-404	8	14
α-helix	407-411	5
β-strand	415-420	6	15
α-helix	428	1
β-strand	429-434	6	15
β-strand	441	1	16
β-strand	444-449	6	17
α-helix	450-452	3
β-strand	453	1	18
β-strand	456	1	18
β-strand	459-469	11	17
β-strand	470	1	16
β-strand	475-476	2	19
β-strand	479	1	19
α-helix	487-489	3
β-strand	491-492	2	17
β-strand	496-497	2	17
β-strand	503-512	10	17
α-helix	513-518	6
β-strand	522-527	6	19
β-strand	536-541	6	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High affinity immunoglobulin epsilon receptor alpha-subunit	A	protein	176	Homo sapiens	P12319 (AlphaFold model)
Ig epsilon chain C region	B, D	protein	222	Homo sapiens	P01854 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1F6A_1 HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT (chains A)
VPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKF
EDSGEYKCQHQQVAESEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIY
YKDGEALKYWYENHAISITNAAAEDSGTYYCTGKVWQLDYESEPLNITVIKAPREK

Sequence of entity 2 (B, D), FASTA

>1F6A_2 IG EPSILON CHAIN C REGION (chains B, D)
ADPCDSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGKPVNHS
TRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPEV
YAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFV
FSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPGK

Ligands and cofactors

ID	Name	Formula	Copies
CPS	3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate	C32 H58 N2 O7 S	5

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc (epsilon) RI (alpha). Garman, S.C., Wurzburg, B.A., Tarchevskaya, S.S. et al. Nature (2000) 406:259-266. DOI 10.1038/35018500 · 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
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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1F6A is part of these collections:

Antibodies and the immune system

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