5HYS: IgE
Structure of IgE complexed with omalizumab. Determined by X-ray diffraction at 2.5 Å resolution. Released 1 Jun 2016.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 20,626
- Mol. weight
- 301.11 kDa
- Released
- 1 Jun 2016
Explore 5HYS in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5HYS contains 108 α-helices and 256 β-strands across 12 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: 8 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 11 |
| β-strand | 10-12 | 3 | 12 |
| β-strand | 18-25 | 8 | 11 |
| β-strand | 34-40 | 7 | 12 |
| β-strand | 46-53 | 8 | 12 |
| β-strand | 58-60 | 3 | 12 |
| β-strand | 68-73 | 6 | 11 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 11 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-102 | 11 | 12 |
| β-strand | 105-111 | 7 | 12 |
| β-strand | 115-119 | 5 | 12 |
| β-strand | 125 | 1 | 13 |
| α-helix | 126-127 | 2 | |
| β-strand | 128-132 | 5 | 14 |
| α-helix | 133-135 | 3 | |
| β-strand | 143-153 | 11 | 14 |
| β-strand | 154 | 1 | 13 |
| β-strand | 159-162 | 4 | 15 |
| α-helix | 163-165 | 3 | |
| β-strand | 167 | 1 | 15 |
| β-strand | 171-173 | 3 | 14 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 14 |
| β-strand | 184-193 | 10 | 14 |
| α-helix | 196-199 | 4 | |
| β-strand | 203-208 | 6 | 15 |
| α-helix | 209-211 | 3 | |
| β-strand | 213-218 | 6 | 15 |
Chain B: 8 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 16 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 16 |
| β-strand | 30-31 | 2 | 17 |
| β-strand | 34-35 | 2 | 17 |
| β-strand | 37-42 | 6 | 2 |
| β-strand | 49-53 | 5 | 2 |
| β-strand | 57-58 | 2 | 2 |
| α-helix | 59 | 1 | |
| β-strand | 66-71 | 6 | 16 |
| β-strand | 74-79 | 6 | 16 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 2 |
| α-helix | 100 | 1 | |
| β-strand | 101-102 | 2 | 2 |
| β-strand | 106-111 | 6 | 2 |
| β-strand | 115 | 1 | 18 |
| α-helix | 116-117 | 2 | |
| β-strand | 118-122 | 5 | 19 |
| α-helix | 123-125 | 3 | |
| α-helix | 128-130 | 3 | |
| β-strand | 133-143 | 11 | 19 |
| β-strand | 144 | 1 | 18 |
| β-strand | 149-154 | 6 | 20 |
| β-strand | 157-158 | 2 | 20 |
| β-strand | 163-167 | 5 | 19 |
| α-helix | 168-171 | 4 | |
| β-strand | 177-186 | 10 | 19 |
| α-helix | 187-192 | 6 | |
| β-strand | 195-201 | 7 | 20 |
| β-strand | 209-214 | 6 | 20 |
Chain C: 7 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 21 |
| β-strand | 10-12 | 3 | 22 |
| β-strand | 18-25 | 8 | 21 |
| β-strand | 34-40 | 7 | 22 |
| β-strand | 46-53 | 8 | 22 |
| β-strand | 58-60 | 3 | 22 |
| β-strand | 68-73 | 6 | 21 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 21 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-102 | 11 | 22 |
| β-strand | 105-111 | 7 | 22 |
| β-strand | 115-119 | 5 | 22 |
| β-strand | 125 | 1 | 23 |
| α-helix | 126-127 | 2 | |
| β-strand | 128-132 | 5 | 24 |
| β-strand | 139-140 | 2 | 24 |
| β-strand | 143-153 | 11 | 24 |
| β-strand | 154 | 1 | 23 |
| β-strand | 159-162 | 4 | 25 |
| α-helix | 163-165 | 3 | |
| β-strand | 167 | 1 | 25 |
| β-strand | 171-173 | 3 | 24 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 24 |
| β-strand | 184-193 | 10 | 24 |
| α-helix | 196-199 | 4 | |
| β-strand | 202-208 | 7 | 25 |
| α-helix | 209-211 | 3 | |
| β-strand | 213-219 | 7 | 25 |
Chain D: 8 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 26 |
| β-strand | 10-14 | 5 | 22 |
| β-strand | 19-25 | 7 | 26 |
| β-strand | 30-31 | 2 | 27 |
| β-strand | 34-35 | 2 | 27 |
| β-strand | 37-42 | 6 | 22 |
| β-strand | 49-53 | 5 | 22 |
| β-strand | 57-58 | 2 | 22 |
| α-helix | 59 | 1 | |
| β-strand | 66-71 | 6 | 26 |
| β-strand | 74-79 | 6 | 26 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 22 |
| α-helix | 100 | 1 | |
| β-strand | 101-102 | 2 | 22 |
| β-strand | 106-111 | 6 | 22 |
| β-strand | 115 | 1 | 28 |
| α-helix | 116-117 | 2 | |
| β-strand | 118-122 | 5 | 29 |
| α-helix | 123-125 | 3 | |
| α-helix | 126-129 | 4 | |
| β-strand | 133-143 | 11 | 29 |
| β-strand | 144 | 1 | 28 |
| β-strand | 148-154 | 7 | 30 |
| β-strand | 157-158 | 2 | 30 |
| β-strand | 163-167 | 5 | 29 |
| α-helix | 168-171 | 4 | |
| β-strand | 177-186 | 10 | 29 |
| α-helix | 187-192 | 6 | |
| β-strand | 195-202 | 8 | 30 |
| β-strand | 209-214 | 6 | 30 |
Chain E: 6 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 31 |
| β-strand | 10-12 | 3 | 22 |
| β-strand | 18-25 | 8 | 31 |
| β-strand | 34-40 | 7 | 22 |
| β-strand | 46-53 | 8 | 22 |
| β-strand | 58-60 | 3 | 22 |
| β-strand | 68-73 | 6 | 31 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 31 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-102 | 11 | 22 |
| β-strand | 105-111 | 7 | 22 |
| β-strand | 115-119 | 5 | 22 |
| β-strand | 125 | 1 | 32 |
| α-helix | 126-127 | 2 | |
| β-strand | 128-132 | 5 | 33 |
| β-strand | 143-153 | 11 | 33 |
| β-strand | 154 | 1 | 32 |
| β-strand | 159-162 | 4 | 34 |
| β-strand | 167 | 1 | 34 |
| β-strand | 171-173 | 3 | 33 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 33 |
| β-strand | 184-193 | 10 | 33 |
| α-helix | 196-199 | 4 | |
| β-strand | 203-208 | 6 | 34 |
| α-helix | 209-211 | 3 | |
| β-strand | 213-218 | 6 | 34 |
Chain F: 8 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 35 |
| β-strand | 10-14 | 5 | 22 |
| β-strand | 19-25 | 7 | 35 |
| β-strand | 30-31 | 2 | 36 |
| β-strand | 34-35 | 2 | 36 |
| β-strand | 37-42 | 6 | 22 |
| β-strand | 49-53 | 5 | 22 |
| β-strand | 57-58 | 2 | 22 |
| α-helix | 59 | 1 | |
| β-strand | 66-71 | 6 | 35 |
| β-strand | 74-79 | 6 | 35 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-94 | 7 | 22 |
| α-helix | 100 | 1 | |
| β-strand | 101-102 | 2 | 22 |
| β-strand | 106-111 | 6 | 22 |
| β-strand | 115 | 1 | 37 |
| α-helix | 116-117 | 2 | |
| β-strand | 118-122 | 5 | 38 |
| α-helix | 123-125 | 3 | |
| α-helix | 126-131 | 6 | |
| β-strand | 133-143 | 11 | 38 |
| β-strand | 144 | 1 | 37 |
| β-strand | 149-154 | 6 | 39 |
| β-strand | 157-158 | 2 | 39 |
| β-strand | 163-167 | 5 | 38 |
| α-helix | 168-171 | 4 | |
| β-strand | 177-186 | 10 | 38 |
| α-helix | 187-192 | 6 | |
| β-strand | 195-201 | 7 | 39 |
| β-strand | 209-214 | 6 | 39 |
Chain G: 11 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 337-340 | 4 | 40 |
| α-helix | 341-344 | 4 | |
| α-helix | 345-349 | 5 | |
| β-strand | 355-363 | 9 | 40 |
| α-helix | 368-370 | 3 | |
| β-strand | 371-376 | 6 | 41 |
| α-helix | 380-383 | 4 | |
| β-strand | 386-391 | 6 | 40 |
| β-strand | 397-404 | 8 | 40 |
| α-helix | 407-412 | 6 | |
| β-strand | 415-421 | 7 | 41 |
| β-strand | 429-434 | 6 | 41 |
| β-strand | 441 | 1 | 42 |
| α-helix | 442-443 | 2 | |
| β-strand | 444-449 | 6 | 43 |
| α-helix | 450-452 | 3 | |
| β-strand | 459-469 | 11 | 43 |
| β-strand | 470 | 1 | 42 |
| β-strand | 475-480 | 6 | 44 |
| β-strand | 483-484 | 2 | 44 |
| α-helix | 485-486 | 2 | |
| α-helix | 487-489 | 3 | |
| β-strand | 490-492 | 3 | 43 |
| α-helix | 493-495 | 3 | |
| β-strand | 496-497 | 2 | 43 |
| β-strand | 503-512 | 10 | 43 |
| α-helix | 513-518 | 6 | |
| β-strand | 522-527 | 6 | 44 |
| β-strand | 536-541 | 6 | 44 |
Chain H: 9 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-40 | 7 | 2 |
| β-strand | 46-53 | 8 | 2 |
| β-strand | 58-60 | 3 | 2 |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-102 | 11 | 2 |
| β-strand | 105-111 | 7 | 2 |
| β-strand | 115-119 | 5 | 2 |
| α-helix | 123-124 | 2 | |
| β-strand | 125 | 1 | 3 |
| α-helix | 126-127 | 2 | |
| β-strand | 128-132 | 5 | 4 |
| α-helix | 136-138 | 3 | |
| β-strand | 139-140 | 2 | 4 |
| β-strand | 143-153 | 11 | 4 |
| β-strand | 154 | 1 | 3 |
| β-strand | 159-162 | 4 | 5 |
| α-helix | 163-165 | 3 | |
| β-strand | 167 | 1 | 5 |
| β-strand | 171-173 | 3 | 4 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 4 |
| β-strand | 184-193 | 10 | 4 |
| α-helix | 196-199 | 4 | |
| β-strand | 203-208 | 6 | 5 |
| α-helix | 209-211 | 3 | |
| β-strand | 213-218 | 6 | 5 |
4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Epididymis luminal protein 214 | A, C, E, H | protein | 222 | Homo sapiens | |
| Uncharacterized protein | B, D, F, L | protein | 218 | Homo sapiens | |
| Ig epsilon chain C region | G, I, J, K | protein | 230 | Homo sapiens | P01854 (AlphaFold model) |
Sequence of entity 1 (A, C, E, H), FASTA
>5HYS_1 Epididymis luminal protein 214 (chains A, C, E, H)
EVQLVESGGGLVQPGGSLRLSCAVSGYSITSGYSWNWIRQAPGKGLEWVASITYDGSTNY
NPSVKGRITISRDDSKNTFYLQMNSLRAEDTAVYYCARGSHYFGHWHFAVWGQGTLVTVS
SASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS
SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
Sequence of entity 2 (B, D, F, L), FASTA
>5HYS_2 Uncharacterized protein (chains B, D, F, L)
DIQLTQSPSSLSASVGDRVTITCRASQSVDYDGDSYMNWYQQKPGKAPKLLIYAASYLES
GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQSHEDPYTFGQGTKVEIKRTVAAPSVF
IFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
STLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 3 (G, I, J, K), FASTA
>5HYS_3 Ig epsilon chain C region (chains G, I, J, K)
ADPAADSNPRCVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVNLTWSRASGKPVNH
STRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPE
VYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFF
VFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPGKAADDDDK
Primary citation
Structural basis of omalizumab therapy and omalizumab-mediated IgE exchange. Pennington, L.F., Tarchevskaya, S., Brigger, D. et al. Nat Commun (2016) 7:11610-11610. DOI 10.1038/ncomms11610 · PubMed
Other PDB entries of the same protein (UniProt P01854 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5MOL 1.75 Å, Human IgE-Fc crystal structure
- 2WQR 1.9 Å, The high resolution crystal structure of IgE Fc
- 5MOK 2.0 Å, Crystal structure of human IgE-Fc epsilon 3-4
- 5MOI 2.2 Å, Crystal structure of human IgE-Fc epsilon 3-4
- 3H9Y 2.23 Å, Crystal structure of the IgE-Fc3-4 domains
- 5MOJ 2.26 Å, Crystal structure of IgE-Fc epsilon 3-4
- 1FP5 2.3 Å, Crystal structure analysis of the human IgE-fc CEPSILON3-CEPSILON4 fragment.
- 30AF 2.4 Å, Complex between IgE-Fc and anti-IgE Fab aeFab98
- 3H9Z 2.45 Å, Crystal structure of the IgE-Fc3-4 domains
- 1O0V 2.6 Å, The crystal structure of IgE Fc reveals an asymmetrically bent conformation
- 5LGJ 2.6 Å, The crystal structure of IgE fc mutant - P333C
- 4GT7 2.61 Å, An engineered disulfide bond reversibly traps the IgE-Fc3-4 in a closed, non-receptor…
Browse structure collections
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