1J88: PDB entry 1J88

Human high affinity fc receptor fc(epsilon)ri(alpha), tetragonal crystal form 1. Determined by X-ray diffraction at 3.2 Å resolution. Released 29 Aug 2001.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 5
Atoms: 7,606
Mol. weight: 110.49 kDa
Ligands: NAG
Released: 29 Aug 2001

Explore 1J88 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1J88 contains 24 α-helices and 110 β-strands across 5 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, 22 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	38-39	2	3
β-strand	40-41	2	4
β-strand	44-45	2	4
α-helix	46	1
β-strand	52-55	4	1
α-helix	60-62	3
β-strand	64-66	3	5
β-strand	68-69	2	3
α-helix	74-78	5
β-strand	79-81	3	5
β-strand	82-84	3	2
β-strand	88-92	5	6
β-strand	96-98	3	7
β-strand	103-104	2	8
β-strand	105-109	5	6
α-helix	110-112	3
β-strand	115-122	8	9
β-strand	125-132	8	9
β-strand	137-138	2	8
β-strand	147-155	9	9
β-strand	158-161	4	9
α-helix	162-164	3
β-strand	165-167	3	9
β-strand	168-170	3	7

Chain B: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	10
β-strand	15-17	3	11
β-strand	22-25	4	10
β-strand	38-39	2	12
β-strand	40-41	2	13
β-strand	44-45	2	13
α-helix	46	1
β-strand	52-55	4	10
α-helix	60-62	3
β-strand	64-66	3	14
β-strand	68-69	2	12
β-strand	79-81	3	14
β-strand	82-84	3	11
β-strand	88-92	5	15
β-strand	96-98	3	16
β-strand	103-104	2	17
β-strand	105-109	5	15
α-helix	110-112	3
β-strand	115-122	8	18
β-strand	125-132	8	18
β-strand	137-138	2	17
α-helix	141-142	2
β-strand	147-155	9	18
β-strand	158-161	4	18
α-helix	162-164	3
β-strand	165-167	3	18
β-strand	168-170	3	16

Chain C: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	19
β-strand	15-17	3	20
β-strand	22-25	4	19
β-strand	38-39	2	21
β-strand	40-41	2	22
β-strand	44-45	2	22
α-helix	46	1
β-strand	52-55	4	19
α-helix	60-62	3
β-strand	64-66	3	23
β-strand	68-69	2	21
α-helix	74-77	4
β-strand	79-81	3	23
β-strand	82-84	3	20
β-strand	88-92	5	24
β-strand	96-98	3	25
β-strand	103-104	2	26
β-strand	105-109	5	24
α-helix	110-112	3
β-strand	115-122	8	27
β-strand	125-132	8	27
β-strand	137-138	2	26
β-strand	147-155	9	27
β-strand	158-161	4	27
α-helix	162-164	3
β-strand	165-167	3	27
β-strand	168-170	3	25

Chain D: 4 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	28
β-strand	15-17	3	29
β-strand	22-25	4	28
β-strand	38-39	2	30
β-strand	40-41	2	31
β-strand	44-45	2	31
α-helix	46	1
β-strand	52-55	4	28
α-helix	60-62	3
β-strand	64-66	3	32
β-strand	68-69	2	30
β-strand	79-81	3	32
β-strand	82-84	3	29
β-strand	88-92	5	33
β-strand	96-98	3	34
β-strand	103-104	2	35
β-strand	105-109	5	33
α-helix	110-112	3
β-strand	115-122	8	36
β-strand	125-132	8	36
β-strand	137-138	2	35
β-strand	147-155	9	36
β-strand	158-161	4	36
α-helix	162-164	3
β-strand	165-167	3	36
β-strand	168-170	3	34

Chain E: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	37
β-strand	15-17	3	38
β-strand	22-25	4	37
β-strand	38-39	2	39
β-strand	40-41	2	40
β-strand	44-45	2	40
α-helix	46	1
β-strand	52-55	4	37
α-helix	60-62	3
β-strand	64-66	3	41
β-strand	68-69	2	39
α-helix	74-76	3
β-strand	79-81	3	41
β-strand	82-84	3	38
β-strand	88-92	5	42
β-strand	96-98	3	43
β-strand	103-104	2	44
β-strand	105-109	5	42
α-helix	110-112	3
β-strand	115-122	8	45
β-strand	125-132	8	45
β-strand	137-138	2	44
β-strand	147-155	9	45
β-strand	158-161	4	45
α-helix	162-164	3
β-strand	165-167	3	45
β-strand	168-170	3	43

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
High affinity immunoglobulin epsilon receptor alpha-subunit	A, B, C, D, E	protein	172	Homo sapiens	P12319 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>1J88_1 HIGH AFFINITY IMMUNOGLOBULIN EPSILON RECEPTOR ALPHA-SUBUNIT (chains A, B, C, D, E)
VPQKPKVSLNPPWNRIFKGENVTLTCNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKF
EDSGEYKCQHQQVNESEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIY
YKDGEALKYWYENHNISITNATVEDSGTYYCTGKVWQLDYESEPLNITVIKA

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	17

Primary citation

The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms. Garman, S.C., Sechi, S., Kinet, J.P. et al. J Mol Biol (2001) 311:1049-1062. DOI 10.1006/jmbi.2001.4929 · 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
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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