Crystal structure of human Fc at 1.80 A. Determined by X-ray diffraction at 1.8 Å resolution. Released 29 Apr 2015.
Explore 4W4N in 3D Show helices and sheets RCSB PDB PDBe
4W4N contains 21 α-helices and 40 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 | 288-289 | 2 | 1 |
| α-helix | 290-292 | 3 | |
| β-strand | 293-294 | 2 | 1 |
| β-strand | 300-307 | 8 | 1 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 2 |
| β-strand | 332-336 | 5 | 2 |
| β-strand | 344 | 1 | 3 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 4 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-359 | 5 | |
| β-strand | 362-372 | 11 | 4 |
| β-strand | 373 | 1 | 3 |
| β-strand | 378-383 | 6 | 5 |
| β-strand | 386-388 | 3 | 5 |
| 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 | 423-428 | 6 | 5 |
| α-helix | 433-435 | 3 | |
| β-strand | 436-441 | 6 | 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 | 288-289 | 2 | 6 |
| α-helix | 290-292 | 3 | |
| β-strand | 293-294 | 2 | 6 |
| β-strand | 300-307 | 8 | 6 |
| α-helix | 310-314 | 5 | |
| β-strand | 319-324 | 6 | 7 |
| β-strand | 332-336 | 5 | 7 |
| α-helix | 339 | 1 | |
| β-strand | 344 | 1 | 8 |
| α-helix | 345-346 | 2 | |
| β-strand | 347-351 | 5 | 9 |
| α-helix | 352-354 | 3 | |
| α-helix | 355-359 | 5 | |
| β-strand | 362-372 | 11 | 9 |
| β-strand | 373 | 1 | 8 |
| β-strand | 378-383 | 6 | 10 |
| β-strand | 386-387 | 2 | 10 |
| 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 | 414-418 | 5 | |
| β-strand | 423-428 | 6 | 10 |
| α-helix | 433-435 | 3 | |
| β-strand | 437-441 | 5 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig gamma-1 chain C region | A, B | protein | 223 | Homo sapiens | P01857 (AlphaFold model) |
>4W4N_1 Ig gamma-1 chain C region (chains A, B) HTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVE VHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQP REPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGS FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPG
Structural basis for binding of human IgG1 to its high-affinity human receptor Fc gamma RI. Kiyoshi, M., Caaveiro, J.M.M., Kawai, T. et al. Nat Commun (2015) 6:6866-6866. DOI 10.1038/ncomms7866 · 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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