Complex of fcgammariia (CD32) and the FC of human IGG1. Determined by X-ray diffraction at 3.8 Å resolution. Released 31 Aug 2011.
Explore 3RY6 in 3D Show helices and sheets RCSB PDB PDBe
3RY6 contains 5 α-helices and 37 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 |
|---|---|---|---|
| α-helix | 248-250 | 3 | |
| β-strand | 347-348 | 2 | 1 |
| β-strand | 351 | 1 | 1 |
| α-helix | 355-358 | 4 | |
| β-strand | 362-370 | 9 | 1 |
| β-strand | 379-382 | 4 | 2 |
| β-strand | 388 | 1 | 2 |
| β-strand | 391-392 | 2 | 1 |
| α-helix | 394-396 | 3 | |
| β-strand | 397 | 1 | 1 |
| β-strand | 405-413 | 9 | 1 |
| α-helix | 414-419 | 6 | |
| β-strand | 424-427 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 344 | 1 | 3 |
| β-strand | 348-349 | 2 | 4 |
| β-strand | 363 | 1 | 5 |
| β-strand | 368-372 | 5 | 4 |
| β-strand | 373 | 1 | 3 |
| β-strand | 379-381 | 3 | 6 |
| β-strand | 382 | 1 | 7 |
| β-strand | 387 | 1 | 7 |
| β-strand | 392-393 | 2 | 8 |
| β-strand | 404-406 | 3 | 4 |
| β-strand | 408-409 | 2 | 8 |
| β-strand | 412 | 1 | 5 |
| β-strand | 423 | 1 | 9 |
| β-strand | 425-427 | 3 | 6 |
| β-strand | 437-438 | 2 | 6 |
| β-strand | 441 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 43 | 1 | 10 |
| β-strand | 48 | 1 | 10 |
| β-strand | 91 | 1 | 11 |
| β-strand | 107-109 | 3 | 12 |
| β-strand | 112 | 1 | 11 |
| α-helix | 113-115 | 3 | |
| β-strand | 118-119 | 2 | 13 |
| β-strand | 123-124 | 2 | 14 |
| β-strand | 130 | 1 | 14 |
| β-strand | 138-140 | 3 | 12 |
| β-strand | 153-154 | 2 | 14 |
| β-strand | 157-158 | 2 | 13 |
| β-strand | 161-162 | 2 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig gamma-1 chain C region | A, B | protein | 214 | Homo sapiens | P01857 (AlphaFold model) |
| Low affinity immunoglobulin gamma Fc region receptor II-a | C | protein | 167 | Homo sapiens | P12318 (AlphaFold model) |
>3RY6_1 Ig gamma-1 chain C region (chains A, B) APELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPQVKFNWYVDGVQVHNAKTK PREQQYNSTYRVVSVLTVLHQNWLDGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYT LPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKL TVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLS
>3RY6_2 Low affinity immunoglobulin gamma Fc region receptor II-a (chains C) KAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDS GEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQN GKSQKFSRLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
Water and common crystallization additives (GOL) are not listed.
Structural Basis for Fc{gamma}RIIa Recognition of Human IgG and Formation of Inflammatory Signaling Complexes. Ramsland, P.A., Farrugia, W., Bradford, T.M. et al. J Immunol (2011) 187:3208-3217. DOI 10.4049/jimmunol.1101467 · PubMed
Other PDB entries of the same protein (UniProt P01857 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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