Crystal structure of the isolated IgG4 CH3 domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 5 Dec 2012.
Explore 4B53 in 3D Show helices and sheets RCSB PDB PDBe
4B53 contains 12 α-helices and 22 β-strands across 2 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 | 344 | 1 | 1 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 2 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-359 | 5 | |
| β-strand | 362-372 | 11 | 2 |
| β-strand | 373 | 1 | 1 |
| β-strand | 378-383 | 6 | 3 |
| β-strand | 386-387 | 2 | 3 |
| β-strand | 391-393 | 3 | 2 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 2 |
| β-strand | 404-413 | 10 | 2 |
| α-helix | 414-418 | 5 | |
| β-strand | 423-428 | 6 | 3 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 344 | 1 | 4 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 5 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-359 | 5 | |
| β-strand | 362-372 | 11 | 5 |
| β-strand | 373 | 1 | 4 |
| β-strand | 378-383 | 6 | 6 |
| β-strand | 386-388 | 3 | 6 |
| β-strand | 391-393 | 3 | 5 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 5 |
| β-strand | 404-413 | 10 | 5 |
| α-helix | 414-418 | 5 | |
| β-strand | 423-428 | 6 | 6 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig gamma-4 chain C region | A, B | protein | 106 | HOMO SAPIENS | P01861 (AlphaFold model) |
>4B53_1 IG GAMMA-4 CHAIN C REGION (chains A, B) QPREPQVYTLPPSQEEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSD GSFFLYSRLTVDKSRWQEGNVFSCSVMHEALHNHYTQKSLSLSLGK
Crystal Structure of the Human Igg4 C(H)3 Dimer Reveals the Role of Arg409 in the Mechanism of Fab-Arm Exchange. Davies, A.M., Rispens, T., Den Bleker, T.H. et al. Mol Immunol (2012) 54:1. DOI 10.1016/J.MOLIMM.2012.10.029 · PubMed
Other PDB entries of the same protein (UniProt P01861 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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