IgE Fv SPE7 complexed with a recombinant thioredoxin. Determined by X-ray diffraction at 2.78 Å resolution. Released 15 Jan 2004.
Explore 1OAZ in 3D Show helices and sheets RCSB PDB PDBe
1OAZ contains 19 α-helices and 67 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-6 | 2 | 1 |
| α-helix | 12 | 1 | |
| α-helix | 13-17 | 5 | |
| β-strand | 22-28 | 7 | 1 |
| β-strand | 35 | 1 | 2 |
| α-helix | 53-56 | 4 | |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 81-84 | 4 | |
| β-strand | 88 | 1 | 2 |
| β-strand | 91-96 | 6 | 1 |
| β-strand | 100-105 | 6 | 1 |
| α-helix | 110-117 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 5 |
| β-strand | 10-12 | 3 | 6 |
| β-strand | 18-25 | 8 | 5 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 7 |
| β-strand | 46-52 | 7 | 7 |
| β-strand | 57-60 | 4 | 7 |
| α-helix | 62-64 | 3 | |
| β-strand | 72-73 | 2 | 5 |
| β-strand | 78-83 | 6 | 5 |
| α-helix | 88-90 | 3 | |
| β-strand | 93-100 | 8 | 7 |
| β-strand | 106-107 | 2 | 7 |
| β-strand | 109 | 1 | 8 |
| β-strand | 114-115 | 2 | 7 |
| β-strand | 116-118 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 9 |
| β-strand | 10-12 | 3 | 10 |
| β-strand | 18-25 | 8 | 9 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-34 | 2 | 11 |
| β-strand | 36-39 | 4 | 12 |
| β-strand | 46-52 | 7 | 12 |
| β-strand | 57-60 | 4 | 12 |
| α-helix | 62-64 | 3 | |
| β-strand | 70-73 | 4 | 9 |
| β-strand | 78-83 | 6 | 9 |
| α-helix | 88-90 | 3 | |
| β-strand | 93-95 | 3 | 12 |
| β-strand | 97-100 | 4 | 11 |
| β-strand | 106-108 | 3 | 11 |
| β-strand | 109 | 1 | 13 |
| β-strand | 110 | 1 | 11 |
| β-strand | 114-115 | 2 | 12 |
| β-strand | 116-118 | 3 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 14 |
| β-strand | 9-12 | 4 | 8 |
| β-strand | 17-22 | 6 | 15 |
| β-strand | 23-24 | 2 | 14 |
| β-strand | 36-41 | 6 | 8 |
| β-strand | 45-51 | 7 | 8 |
| β-strand | 55-56 | 2 | 8 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 15 |
| β-strand | 72-78 | 7 | 15 |
| β-strand | 87-94 | 8 | 8 |
| β-strand | 97-100 | 4 | 8 |
| β-strand | 105-108 | 4 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 16 |
| β-strand | 9-12 | 4 | 13 |
| β-strand | 17-22 | 6 | 17 |
| β-strand | 23-24 | 2 | 16 |
| β-strand | 36-41 | 6 | 13 |
| β-strand | 45-51 | 7 | 13 |
| β-strand | 55-56 | 2 | 13 |
| α-helix | 57 | 1 | |
| β-strand | 64-69 | 6 | 17 |
| β-strand | 72-78 | 7 | 17 |
| α-helix | 82-84 | 3 | |
| β-strand | 87-94 | 8 | 13 |
| β-strand | 97-100 | 4 | 13 |
| β-strand | 105-108 | 4 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Thioredoxin 1 | A, B | protein | 123 | ESCHERICHIA COLI | P0AA25 (AlphaFold model) |
| Immunoglobulin E | H, J | protein | 122 | MUS MUSCULUS | |
| Immunoglobulin E | L, N | protein | 110 | MUS MUSCULUS | P01724 (AlphaFold model) |
>1OAZ_1 THIOREDOXIN 1 (chains A, B) MSDKIIHLTDDSFDTDVLKADGAILVDFWAEWCGPIEESDDRRYDLVGPCKMIAPILDEI ADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDA NLA
>1OAZ_2 IMMUNOGLOBULIN E (chains H, J) EVQLQQSGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNGGGTKY NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCARMWYYGTYYFDYWGQGTTLTVSS AA
>1OAZ_3 IMMUNOGLOBULIN E (chains L, N) QAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGV PARFSGSLIGNKAALTITGAQTEDEAIYFCALWYSNHLVFGGGTKLTVLT
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 P0AA25 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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