2Y7Q: PDB entry 2Y7Q

The high-affinity complex between IgE and its receptor fc epsilon ri. Determined by X-ray diffraction at 3.4 Å resolution. Released 20 Apr 2011.

Method: X-ray diffraction
Resolution: 3.4 Å
Organism: HOMO SAPIENS
Chains: 3
Atoms: 5,355
Mol. weight: 95.84 kDa
Ligands: NAG
Released: 20 Apr 2011

Explore 2Y7Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Y7Q contains 22 α-helices and 66 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, 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	38-42	5	3
β-strand	44-46	3	3
β-strand	52-55	4	1
α-helix	60-62	3
β-strand	64-69	6	3
β-strand	76-81	6	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	113-114	2
β-strand	115-122	8	6
β-strand	125-130	6	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	168-169	2	5

Chain B: 10 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	230-232	3
β-strand	233-239	7	7
β-strand	250-259	11	7
β-strand	264-270	7	8
β-strand	273-280	8	8
β-strand	291-300	10	7
α-helix	301-304	4
β-strand	310-316	7	8
β-strand	320-325	6	8
α-helix	328-330	3
α-helix	333-335	3
β-strand	337-340	4	9
α-helix	341-344	4
α-helix	345	1
α-helix	346-350	5
β-strand	355-363	9	9
α-helix	364-365	2
β-strand	371-376	6	10
β-strand	388-391	4	9
β-strand	397-404	8	9
α-helix	407-411	5
β-strand	415	1	11
β-strand	416-421	6	10
β-strand	429-431	3	10
β-strand	434	1	11
β-strand	444	1	12
β-strand	447-449	3	12
β-strand	461-467	7	12
β-strand	474-478	5	13
β-strand	490-492	3	12
α-helix	493-495	3
β-strand	504-510	7	12
β-strand	523-528	6	13
β-strand	537-540	4	13

Chain D: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	231-232	2
β-strand	233-239	7	7
β-strand	250-259	11	7
β-strand	264-270	7	14
β-strand	273-280	8	14
β-strand	291-300	10	7
α-helix	301-305	5
β-strand	310-314	5	14
β-strand	321-325	5	14
β-strand	337-340	4	15
α-helix	341-344	4
α-helix	345	1
α-helix	346-350	5
β-strand	355-363	9	15
β-strand	371-376	6	16
α-helix	384-385	2
β-strand	386	1	15
β-strand	389	1	15
β-strand	397-404	8	15
α-helix	407-411	5
β-strand	415-421	7	16
β-strand	429-434	6	16
β-strand	444	1	17
β-strand	447-449	3	17
β-strand	462-469	8	17
β-strand	474-479	6	18
β-strand	490-492	3	17
α-helix	493-495	3
β-strand	503-509	7	17
β-strand	523-528	6	18
β-strand	537-540	4	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High affinity immunoglobulin epsilon receptor subunit alpha	A	protein	188	HOMO SAPIENS	P12319 (AlphaFold model)
Ig epsilon chain C region	B, D	protein	327	HOMO SAPIENS	P01854 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2Y7Q_1 HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR SUBUNIT ALPHA (chains A)
ETGVPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVSSTKWFHNGSLSEETNSSLNIVN
AKFEDSGEYKCQHQQVAESEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYK
VIYYKDGEALKYWYENHAISITNAAAEDSGTYYCTGKVWQLDYESEPLNITVIKAPREKG
TKHHHHHH

Sequence of entity 2 (B, D), FASTA

>2Y7Q_2 IG EPSILON CHAIN C REGION (chains B, D)
DIVASRDFTPPTVKILQSSCDGGGHFPPTIQLLCLVSGYTPGTIQITWLEDGQVMDVDLS
TASTTQEGELASTQSELTLSQKHWLSDRTYTCQVTYQGHTFEDSTKKCADSNPRGVSAYL
SRPSPFDLFIRKSPTITCLVVDLAPSKGTVQLTWSRASGKPVNHSTRKEEKQRNGTLTVT
STLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPEVYAFATPEWPGSRDKR
TLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKD
EFICRAVHEAASPSQTVQRAVSVNPGK

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3

Primary citation

Conformational Changes in Ige Contribute to its Uniquely Slow Dissociation Rate from Receptor Fceri. Holdom, M.D., Davies, A.M., Nettleship, J.E. et al. Nat Struct Mol Biol (2011) 18:571. DOI 10.1038/NSMB.2044 · 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
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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