Crystal structure of mouse IgG2a Fc T370K mutant. Determined by X-ray diffraction at 1.55 Å resolution. Released 7 Jun 2017.
Explore 5VAA in 3D Show helices and sheets RCSB PDB PDBe
5VAA contains 21 α-helices and 38 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 | 239-243 | 5 | 1 |
| α-helix | 244-246 | 3 | |
| α-helix | 247-251 | 5 | |
| β-strand | 258-266 | 9 | 1 |
| β-strand | 274-279 | 6 | 2 |
| β-strand | 282-284 | 3 | 2 |
| β-strand | 288-294 | 7 | 1 |
| β-strand | 299-307 | 9 | 1 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 2 |
| β-strand | 332-336 | 5 | 2 |
| α-helix | 338-340 | 3 | |
| β-strand | 344 | 1 | 3 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 4 |
| α-helix | 355-359 | 5 | |
| β-strand | 362-372 | 11 | 4 |
| β-strand | 373 | 1 | 3 |
| β-strand | 378-383 | 6 | 5 |
| β-strand | 386-387 | 2 | 5 |
| α-helix | 388 | 1 | |
| β-strand | 391-393 | 3 | 4 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 4 |
| β-strand | 404-413 | 10 | 4 |
| α-helix | 414-418 | 5 | |
| β-strand | 424-428 | 5 | 5 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-440 | 5 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 239-243 | 5 | 6 |
| α-helix | 244-246 | 3 | |
| α-helix | 247-251 | 5 | |
| β-strand | 258-266 | 9 | 6 |
| β-strand | 274-279 | 6 | 7 |
| β-strand | 282-284 | 3 | 7 |
| β-strand | 288-294 | 7 | 6 |
| β-strand | 299-307 | 9 | 6 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 7 |
| β-strand | 332-336 | 5 | 7 |
| α-helix | 338-340 | 3 | |
| β-strand | 344 | 1 | 8 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 9 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-357 | 3 | |
| β-strand | 362-372 | 11 | 9 |
| β-strand | 373 | 1 | 8 |
| β-strand | 378-383 | 6 | 10 |
| β-strand | 386-387 | 2 | 10 |
| α-helix | 388 | 1 | |
| β-strand | 391-393 | 3 | 9 |
| α-helix | 394-396 | 3 | |
| β-strand | 397-398 | 2 | 9 |
| β-strand | 404-413 | 10 | 9 |
| α-helix | 414-420 | 7 | |
| β-strand | 423-428 | 6 | 10 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-439 | 4 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig gamma-2A chain C region, A allele | A, B | protein | 226 | Mus musculus | P01863 (AlphaFold model) |
>5VAA_1 Ig gamma-2A chain C region, A allele (chains A, B) GSCPPCKCPAPNLLGGPSVFIFPPKIKDVLMISLSPIVTCVVVDVSEDDPDVQISWFVNN VEVHTAQTQTHREDYNSTLRVVSALPIQHQDWMSGKEFKCKVNNKDLPAPIERTISKPKG SVRAPQVYVLPPPEEEMTKKQVTLTCMVKDFMPEDIYVEWTNNGKTELNYKNTEPVLDSD GSYFMYSKLRVEKKNWVERNSYSCSVVHEGLHNHHTTKSFSRTPGK
Efficient Generation of Bispecific Murine Antibodies for Pre-Clinical Investigations in Syngeneic Rodent Models. Labrijn, A.F., Meesters, J.I., Bunce, M. et al. Sci Rep (2017) 7:2476-2476. DOI 10.1038/s41598-017-02823-9 · PubMed
Other PDB entries of the same protein (UniProt P01863 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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