9EQ3: IgE HMM5
Structure of IgE HMM5 bound to FceRIa cryo-EM class 8. Determined by electron microscopy at 6.9 Å resolution. Released 10 Apr 2024.
- Method
- Electron microscopy
- Resolution
- 6.9 Å
- Organism
- Homo sapiens
- Chains
- 5
- Atoms
- 13,588
- Mol. weight
- 195.24 kDa
- Ligands
- NAG
- Released
- 10 Apr 2024
Explore 9EQ3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9EQ3 contains 61 α-helices and 157 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 H: 20 helices, 48 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 17-24 | 8 | 1 |
| β-strand | 32-38 | 7 | 3 |
| β-strand | 45-50 | 6 | 3 |
| β-strand | 56-58 | 3 | 3 |
| β-strand | 66-70 | 5 | 1 |
| β-strand | 75-80 | 6 | 1 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-96 | 8 | 3 |
| β-strand | 106 | 1 | 3 |
| β-strand | 110-112 | 3 | 3 |
| β-strand | 113 | 1 | 2 |
| β-strand | 120 | 1 | 4 |
| α-helix | 121-122 | 2 | |
| β-strand | 123-127 | 5 | 5 |
| α-helix | 131-133 | 3 | |
| β-strand | 140-150 | 11 | 5 |
| β-strand | 151 | 1 | 4 |
| β-strand | 156-160 | 5 | 6 |
| β-strand | 166-170 | 5 | 5 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-175 | 2 | 5 |
| β-strand | 182-191 | 10 | 5 |
| β-strand | 199-204 | 6 | 6 |
| β-strand | 213-218 | 6 | 6 |
| α-helix | 226-228 | 3 | |
| β-strand | 230-235 | 6 | 7 |
| α-helix | 236-237 | 2 | |
| α-helix | 242-244 | 3 | |
| β-strand | 246-256 | 11 | 7 |
| β-strand | 261-267 | 7 | 8 |
| β-strand | 270-271 | 2 | 8 |
| α-helix | 272-273 | 2 | |
| α-helix | 274-276 | 3 | |
| β-strand | 277-284 | 8 | 7 |
| β-strand | 287-297 | 11 | 7 |
| α-helix | 298-302 | 5 | |
| β-strand | 307-313 | 7 | 8 |
| β-strand | 316-322 | 7 | 8 |
| β-strand | 334-337 | 4 | 9 |
| α-helix | 338-341 | 4 | |
| α-helix | 342-346 | 5 | |
| β-strand | 352-360 | 9 | 9 |
| α-helix | 366-367 | 2 | |
| β-strand | 368-373 | 6 | 10 |
| α-helix | 377-382 | 6 | |
| β-strand | 383-388 | 6 | 9 |
| β-strand | 394-401 | 8 | 9 |
| α-helix | 404-408 | 5 | |
| β-strand | 413-418 | 6 | 10 |
| β-strand | 426-430 | 5 | 10 |
| β-strand | 438 | 1 | 11 |
| α-helix | 439-440 | 2 | |
| β-strand | 441-446 | 6 | 12 |
| α-helix | 447-449 | 3 | |
| β-strand | 456-466 | 11 | 12 |
| β-strand | 467 | 1 | 11 |
| β-strand | 471-477 | 7 | 13 |
| β-strand | 481 | 1 | 13 |
| α-helix | 484-486 | 3 | |
| β-strand | 487-489 | 3 | 12 |
| α-helix | 490-492 | 3 | |
| β-strand | 493-494 | 2 | 12 |
| β-strand | 500-509 | 10 | 12 |
| α-helix | 510-515 | 6 | |
| β-strand | 518-525 | 8 | 13 |
| β-strand | 533-539 | 7 | 13 |
Chain L: 9 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 14 |
| β-strand | 10 | 1 | 15 |
| β-strand | 18-25 | 8 | 14 |
| α-helix | 28-29 | 2 | |
| α-helix | 30-32 | 3 | |
| β-strand | 35-40 | 6 | 15 |
| β-strand | 47-51 | 5 | 15 |
| β-strand | 55-56 | 2 | 15 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 14 |
| β-strand | 72-78 | 7 | 14 |
| α-helix | 82-84 | 3 | |
| β-strand | 87-94 | 8 | 15 |
| β-strand | 98-101 | 4 | 15 |
| β-strand | 106 | 1 | 15 |
| β-strand | 114 | 1 | 16 |
| α-helix | 115-116 | 2 | |
| β-strand | 117-121 | 5 | 17 |
| α-helix | 122-124 | 3 | |
| α-helix | 125-128 | 4 | |
| β-strand | 132-142 | 11 | 17 |
| β-strand | 143 | 1 | 16 |
| β-strand | 148-153 | 6 | 18 |
| β-strand | 156-157 | 2 | 18 |
| β-strand | 162-166 | 5 | 17 |
| α-helix | 168-170 | 3 | |
| β-strand | 176-185 | 10 | 17 |
| α-helix | 186-190 | 5 | |
| β-strand | 194-200 | 7 | 18 |
| β-strand | 208-213 | 6 | 18 |
Chain R: 5 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 19 |
| β-strand | 15-17 | 3 | 20 |
| β-strand | 22-27 | 6 | 19 |
| β-strand | 38-42 | 5 | 21 |
| β-strand | 44-46 | 3 | 21 |
| β-strand | 52-55 | 4 | 19 |
| α-helix | 60-62 | 3 | |
| β-strand | 64-69 | 6 | 21 |
| β-strand | 79-81 | 3 | 21 |
| β-strand | 82-84 | 3 | 20 |
| β-strand | 88-92 | 5 | 22 |
| β-strand | 96-98 | 3 | 23 |
| β-strand | 103-109 | 7 | 22 |
| α-helix | 110-112 | 3 | |
| α-helix | 113-114 | 2 | |
| β-strand | 115-122 | 8 | 24 |
| β-strand | 125-130 | 6 | 24 |
| β-strand | 135-138 | 4 | 22 |
| α-helix | 143-145 | 3 | |
| β-strand | 147-155 | 9 | 24 |
| β-strand | 158-161 | 4 | 24 |
| α-helix | 162-164 | 3 | |
| β-strand | 165-167 | 3 | 24 |
| β-strand | 168-170 | 3 | 23 |
Chain X: 17 helices, 48 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 25 |
| β-strand | 10-11 | 2 | 26 |
| β-strand | 17-24 | 8 | 25 |
| β-strand | 32-38 | 7 | 27 |
| β-strand | 45-50 | 6 | 27 |
| β-strand | 56-58 | 3 | 27 |
| β-strand | 66-70 | 5 | 25 |
| β-strand | 75-80 | 6 | 25 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-96 | 8 | 27 |
| β-strand | 106 | 1 | 27 |
| β-strand | 110-112 | 3 | 27 |
| β-strand | 113-114 | 2 | 26 |
| β-strand | 120 | 1 | 28 |
| α-helix | 121-122 | 2 | |
| β-strand | 123-127 | 5 | 29 |
| β-strand | 140-150 | 11 | 29 |
| β-strand | 151 | 1 | 28 |
| β-strand | 156-160 | 5 | 30 |
| β-strand | 167-170 | 4 | 29 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-175 | 2 | 29 |
| β-strand | 182-191 | 10 | 29 |
| β-strand | 199-204 | 6 | 30 |
| β-strand | 213-218 | 6 | 30 |
| β-strand | 229-235 | 7 | 7 |
| α-helix | 236-237 | 2 | |
| α-helix | 242-244 | 3 | |
| β-strand | 246-256 | 11 | 7 |
| β-strand | 261-267 | 7 | 31 |
| β-strand | 270-271 | 2 | 31 |
| α-helix | 272-273 | 2 | |
| α-helix | 274-276 | 3 | |
| β-strand | 277-284 | 8 | 7 |
| β-strand | 287-297 | 11 | 7 |
| α-helix | 298-302 | 5 | |
| β-strand | 307-313 | 7 | 31 |
| β-strand | 316-322 | 7 | 31 |
| β-strand | 334-337 | 4 | 32 |
| α-helix | 338-341 | 4 | |
| α-helix | 342-346 | 5 | |
| β-strand | 352-360 | 9 | 32 |
| β-strand | 368-373 | 6 | 33 |
| β-strand | 383-388 | 6 | 32 |
| β-strand | 394-401 | 8 | 32 |
| α-helix | 404-408 | 5 | |
| β-strand | 413-418 | 6 | 33 |
| β-strand | 426-430 | 5 | 33 |
| β-strand | 438 | 1 | 34 |
| α-helix | 439-440 | 2 | |
| β-strand | 441-446 | 6 | 35 |
| α-helix | 447-450 | 4 | |
| β-strand | 456-466 | 11 | 35 |
| β-strand | 467 | 1 | 34 |
| β-strand | 471-477 | 7 | 36 |
| β-strand | 480-481 | 2 | 36 |
| α-helix | 482-483 | 2 | |
| α-helix | 484-486 | 3 | |
| β-strand | 487-489 | 3 | 35 |
| α-helix | 490-492 | 3 | |
| β-strand | 493-494 | 2 | 35 |
| β-strand | 500-509 | 10 | 35 |
| α-helix | 510-515 | 6 | |
| β-strand | 519-525 | 7 | 36 |
| β-strand | 533-538 | 6 | 36 |
Chain Y: 10 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 37 |
| β-strand | 10-13 | 4 | 38 |
| β-strand | 19-25 | 7 | 37 |
| α-helix | 28-29 | 2 | |
| α-helix | 30-32 | 3 | |
| β-strand | 35-40 | 6 | 38 |
| β-strand | 47-51 | 5 | 38 |
| β-strand | 55-56 | 2 | 38 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 37 |
| β-strand | 72-77 | 6 | 37 |
| α-helix | 82-84 | 3 | |
| β-strand | 87-94 | 8 | 38 |
| β-strand | 98-101 | 4 | 38 |
| β-strand | 105-109 | 5 | 38 |
| β-strand | 114 | 1 | 39 |
| α-helix | 115-116 | 2 | |
| β-strand | 117-121 | 5 | 40 |
| α-helix | 122-124 | 3 | |
| α-helix | 125-128 | 4 | |
| β-strand | 132-142 | 11 | 40 |
| β-strand | 143 | 1 | 39 |
| β-strand | 147-153 | 7 | 41 |
| β-strand | 156-157 | 2 | 41 |
| α-helix | 158 | 1 | |
| β-strand | 162-166 | 5 | 40 |
| α-helix | 167-170 | 4 | |
| β-strand | 176-185 | 10 | 40 |
| α-helix | 186-190 | 5 | |
| β-strand | 194-201 | 8 | 41 |
| β-strand | 208-213 | 6 | 41 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| IgE HMM5 heavy chain | H, X | protein | 551 | Homo sapiens | |
| IgE HMM5 light chain | L, Y | protein | 217 | Homo sapiens | |
| High affinity immunoglobulin epsilon receptor subunit alpha | R | protein | 171 | Homo sapiens | P12319 (AlphaFold model) |
Sequence of entity 1 (H, X), FASTA
>9EQ3_1 IgE HMM5 heavy chain (chains H, X)
QSLEESGGRLVTPGTPLTLTCTVSGFSLSTYNIHWVRQAPGKGLEWIGVIDTGGGTYFAS
WAKGRFAISKTSSTTVDLKMTSLTAADTATYFCAKGFDYSASTNLWGPGTLVTISSASTQ
SPSVFPLTRCCKNIPSNATSVTLGCLATGYFPEPVMVTWDTGSLNGTTMTLPATTLTLSG
HYATISLLTVSGAWAKQMFTCRVAHTPSSTDWVDNKTFSVCSRDFTPPTVKILQSSCDGG
GHFPPTIQLLCLVSGYTPGTINITWLEDGQVMDVDLSTASTTQEGELASTQSELTLSQKH
WLSDRTYTCQVTYQGHTFEDSTKKCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDL
APSKGTVNLTWSRASGKPVNHSTRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHP
HLPRALMRSTTKTSGPRAAPEVYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEV
QLPDARHSTTQPRKTKGSGFFVFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSS
VNPGKHHHHHH
Sequence of entity 2 (L, Y), FASTA
>9EQ3_2 IgE HMM5 light chain (chains L, Y)
ELDMTQTPSSVSAPVGGSVTINCQSSQSVYGNNYLAWYQQKAGQPPKLLIYRASTLASGA
PSRFKGSGSGTQFTLTISDLESDDAATYYCLGYYNGVINVFGGGTNVEIKRTVGAPSVFI
FPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSS
TLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (R), FASTA
>9EQ3_3 High affinity immunoglobulin epsilon receptor subunit alpha (chains R)
KPKVSLNPPWNRIFKGENVTLTCNGNNFFEVSSTKWFHNGSLSEETNSSLNIVNAKFEDS
GEYKCQHQQVNESEPVYLEVFSDWLLLQASAEVVMEGQPLFLRCHGWRNWDVYKVIYYKD
GEALKYWYENHNISITNATVEDSGTYYCTGKVWQLDYESEPLNITVIKAPR
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 8 |
Primary citation
The dynamics of hinge flexibility in receptor bound immunoglobulin E revealed by electron microscopy. Jensen, R.K., Miehe, M., Gandini, R. et al. bioRxiv (2023). DOI 10.1101/2023.02.17.528943
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)
- 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
Browse structure collections
About this viewer
MolViewer shows 9EQ3 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.