1OAY: Immunoglobulin E
Antibody multispecificity mediated by conformational diversity. Determined by X-ray diffraction at 2.66 Å resolution. Released 15 Jan 2004.
- Method
- X-ray diffraction
- Resolution
- 2.66 Å
- Organism
- MUS MUSCULUS
- Chains
- 6
- Atoms
- 5,134
- Mol. weight
- 74.08 kDa
- Ligands
- FUR
- Released
- 15 Jan 2004
Explore 1OAY in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1OAY contains 6 α-helices and 76 β-strands across 6 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: 2 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 18-20 | 3 | 3 |
| β-strand | 22-25 | 4 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 4 |
| β-strand | 47-52 | 6 | 4 |
| β-strand | 57-60 | 4 | 4 |
| β-strand | 70-73 | 4 | 3 |
| β-strand | 78-83 | 6 | 3 |
| α-helix | 88-90 | 3 | |
| β-strand | 93-100 | 8 | 4 |
| β-strand | 106-108 | 3 | 4 |
| β-strand | 109 | 1 | 5 |
| β-strand | 110 | 1 | 4 |
| β-strand | 114-115 | 2 | 4 |
| β-strand | 116-118 | 3 | 2 |
Chain J: 2 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-6 | 4 | 6 |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18-20 | 3 | 8 |
| β-strand | 22-25 | 4 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 9 |
| β-strand | 46-52 | 7 | 9 |
| β-strand | 57-60 | 4 | 9 |
| β-strand | 70-73 | 4 | 8 |
| β-strand | 78-83 | 6 | 8 |
| α-helix | 88-90 | 3 | |
| β-strand | 93-100 | 8 | 9 |
| β-strand | 106-108 | 3 | 9 |
| β-strand | 109 | 1 | 10 |
| β-strand | 110 | 1 | 9 |
| β-strand | 114-115 | 2 | 9 |
| β-strand | 116-118 | 3 | 7 |
Chain L: 1 helix, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-10 | 2 | 11 |
| β-strand | 18-23 | 6 | 12 |
| β-strand | 36-41 | 6 | 5 |
| β-strand | 45-51 | 7 | 5 |
| β-strand | 55-56 | 2 | 5 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 12 |
| β-strand | 72-77 | 6 | 12 |
| β-strand | 87-93 | 7 | 5 |
| β-strand | 98-100 | 3 | 5 |
| β-strand | 105-106 | 2 | 11 |
Chain M: 0 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 13 |
| β-strand | 17-18 | 2 | 14 |
| β-strand | 24 | 1 | 13 |
| β-strand | 37-40 | 4 | 15 |
| β-strand | 41 | 1 | 16 |
| β-strand | 45 | 1 | 16 |
| β-strand | 48 | 1 | 15 |
| β-strand | 64-69 | 6 | 14 |
| β-strand | 72-78 | 7 | 14 |
| β-strand | 87-90 | 4 | 15 |
Chain N: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 17 |
| β-strand | 9-12 | 4 | 18 |
| β-strand | 18-23 | 6 | 19 |
| β-strand | 24 | 1 | 17 |
| β-strand | 36-41 | 6 | 10 |
| β-strand | 45-51 | 7 | 10 |
| β-strand | 55-56 | 2 | 10 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 19 |
| β-strand | 72-77 | 6 | 19 |
| β-strand | 87-93 | 7 | 10 |
| β-strand | 98-100 | 3 | 10 |
| β-strand | 105-108 | 4 | 18 |
Chain O: 0 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 20 |
| β-strand | 12 | 1 | 21 |
| β-strand | 17-18 | 2 | 22 |
| β-strand | 24 | 1 | 20 |
| β-strand | 37 | 1 | 23 |
| β-strand | 38-40 | 3 | 24 |
| β-strand | 41 | 1 | 25 |
| β-strand | 45 | 1 | 25 |
| β-strand | 50 | 1 | 23 |
| β-strand | 56 | 1 | 23 |
| β-strand | 64-69 | 6 | 22 |
| β-strand | 72-78 | 7 | 22 |
| β-strand | 87-89 | 3 | 24 |
| β-strand | 108 | 1 | 21 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Immunoglobulin E | H, J | protein | 122 | MUS MUSCULUS | |
| Immunoglobulin E | L, M, N, O | protein | 110 | MUS MUSCULUS | P01724 (AlphaFold model) |
Sequence of entity 1 (H, J), FASTA
>1OAY_1 IMMUNOGLOBULIN E (chains H, J)
EVQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNGGGTKY
NLKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARMWYYGTYYFDYWGQGTTLTVSS
AA
Sequence of entity 2 (L, M, N, O), FASTA
>1OAY_2 IMMUNOGLOBULIN E (chains L, M, N, O)
QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPRHLFTGLIGGTNNRAPGV
PARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHLVFGGGTKLTVLT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| FUR | Furazolidone | C8 H5 N3 O5 | 2 |
Primary citation
Antibody Multispecificity Mediated by Conformational Diversity. James, L.C., Roversi, P., Tawfik, D. Science (2003) 299:1362. DOI 10.1126/SCIENCE.1079731 · PubMed
Other PDB entries of the same protein (UniProt P01724 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1OAQ 1.5 Å, Free conformation Ab1 of the IgE SPE-7
- 1A6V 1.8 Å, B1-8 FV fragment complexed with a (4-hydroxy-3-nitrophenyl) acetate compound
- 1OAU 1.8 Å, Fv Structure of the IgE SPE-7 in complex with DNP-Ser (immunising hapten)
- 1A6W 2.0 Å, B1-8 fv fragment complexed with a (4-hydroxy-5-iodo-3-nitrophenyl) acetate compound
- 1OCW 2.0 Å, Free conformation Ab2 of the IgE SPE-7
- 1Q0Y 2.0 Å, Anti-Morphine Antibody 9B1 Complexed with Morphine
- 1A6U 2.1 Å, B1-8 fv fragment
- 2BJM 2.15 Å, SPE7:Anthrone Complex
- 1OAR 2.23 Å, Fv IgE SPE-7 in complex with Alizarin Red
- 1DL7 2.35 Å, The structural basis of repertoire shift in an immune response to phosphocholine
- 1OAX 2.67 Å, Fv Structure of the IgE SPE-7 in complex with acenaphthenequinone
- 1OAZ 2.78 Å, IgE Fv SPE7 complexed with a recombinant thioredoxin
Browse structure collections
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