Crystal structure of the IgE-Fc3-4 domains. Determined by X-ray diffraction at 2.23 Å resolution. Released 8 Sept 2009.
Explore 3H9Y in 3D Show helices and sheets RCSB PDB PDBe
3H9Y contains 33 α-helices and 56 β-strands across 3 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 | 337-340 | 4 | 1 |
| α-helix | 341-344 | 4 | |
| α-helix | 345 | 1 | |
| α-helix | 346-351 | 6 | |
| β-strand | 355-361 | 7 | 1 |
| β-strand | 371-376 | 6 | 2 |
| α-helix | 380-385 | 6 | |
| β-strand | 386-392 | 7 | 1 |
| β-strand | 396-404 | 9 | 1 |
| α-helix | 407-412 | 6 | |
| β-strand | 416-421 | 6 | 2 |
| β-strand | 430-433 | 4 | 2 |
| α-helix | 435-437 | 3 | |
| β-strand | 441 | 1 | 3 |
| α-helix | 442-443 | 2 | |
| β-strand | 444-449 | 6 | 4 |
| α-helix | 450-452 | 3 | |
| β-strand | 459-469 | 11 | 4 |
| β-strand | 470 | 1 | 3 |
| β-strand | 475-480 | 6 | 5 |
| β-strand | 483-484 | 2 | 5 |
| α-helix | 485-486 | 2 | |
| α-helix | 487-489 | 3 | |
| β-strand | 490-492 | 3 | 4 |
| α-helix | 493-495 | 3 | |
| β-strand | 496-497 | 2 | 4 |
| β-strand | 503-512 | 10 | 4 |
| α-helix | 513-518 | 6 | |
| β-strand | 522-527 | 6 | 5 |
| β-strand | 536-541 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 336-341 | 6 | 6 |
| α-helix | 342-344 | 3 | |
| α-helix | 345 | 1 | |
| α-helix | 346-351 | 6 | |
| β-strand | 355-362 | 8 | 6 |
| β-strand | 371-376 | 6 | 7 |
| α-helix | 380-384 | 5 | |
| β-strand | 388-391 | 4 | 6 |
| β-strand | 397-404 | 8 | 6 |
| α-helix | 407-411 | 5 | |
| β-strand | 416-421 | 6 | 7 |
| β-strand | 429-433 | 5 | 7 |
| β-strand | 441 | 1 | 8 |
| α-helix | 442-443 | 2 | |
| β-strand | 444-449 | 6 | 9 |
| α-helix | 450-452 | 3 | |
| β-strand | 453 | 1 | 10 |
| β-strand | 456 | 1 | 10 |
| β-strand | 459-469 | 11 | 9 |
| β-strand | 470 | 1 | 8 |
| β-strand | 475-480 | 6 | 11 |
| β-strand | 483-484 | 2 | 11 |
| α-helix | 485-486 | 2 | |
| α-helix | 487-489 | 3 | |
| β-strand | 490-492 | 3 | 9 |
| α-helix | 493-495 | 3 | |
| β-strand | 496-497 | 2 | 9 |
| β-strand | 503-512 | 10 | 9 |
| α-helix | 513-518 | 6 | |
| β-strand | 522-527 | 6 | 11 |
| β-strand | 536-541 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 337-340 | 4 | 12 |
| α-helix | 345 | 1 | |
| α-helix | 346-351 | 6 | |
| β-strand | 355-362 | 8 | 12 |
| β-strand | 371-376 | 6 | 13 |
| α-helix | 380-382 | 3 | |
| β-strand | 386-391 | 6 | 12 |
| α-helix | 396 | 1 | |
| β-strand | 397-404 | 8 | 12 |
| α-helix | 407-411 | 5 | |
| β-strand | 415-421 | 7 | 13 |
| β-strand | 429-434 | 6 | 13 |
| β-strand | 441 | 1 | 14 |
| α-helix | 442-443 | 2 | |
| β-strand | 444-449 | 6 | 15 |
| β-strand | 459-469 | 11 | 15 |
| β-strand | 470 | 1 | 14 |
| β-strand | 475-480 | 6 | 16 |
| β-strand | 483-484 | 2 | 16 |
| α-helix | 485-486 | 2 | |
| α-helix | 487-489 | 3 | |
| β-strand | 490-492 | 3 | 15 |
| α-helix | 493-495 | 3 | |
| β-strand | 496-497 | 2 | 15 |
| β-strand | 503-512 | 10 | 15 |
| α-helix | 513-518 | 6 | |
| β-strand | 522-527 | 6 | 16 |
| β-strand | 536-541 | 6 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig epsilon chain C region | A, B, E | protein | 223 | Homo sapiens | P01854 (AlphaFold model) |
>3H9Y_1 Ig epsilon chain C region (chains A, B, E) ADPCADSNPRGVSAYLSRPSPFDLFIRKSPTITCLVVDLAPSKGTVQLTWSRASGKPVQH STRKEEKQRNGTLTVTSTLPVGTRDWIEGETYQCRVTHPHLPRALMRSTTKTSGPRAAPE VYAFATPEWPGSRDKRTLACLIQNFMPEDISVQWLHNEVQLPDARHSTTQPRKTKGSGFF VFSRLEVTRAEWEQKDEFICRAVHEAASPSQTVQRAVSVNPGK
Conformational flexibility in immunoglobulin E-Fc 3-4 revealed in multiple crystal forms. Wurzburg, B.A., Jardetzky, T.S. J Mol Biol (2009) 393:176-190. DOI 10.1016/j.jmb.2009.08.012 · PubMed
Other PDB entries of the same protein (UniProt P01854 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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