Crystal structure of human IgD-Fc. Determined by X-ray diffraction at 3.0 Å resolution. Released 4 Dec 2024.
Explore 9FMB in 3D Show helices and sheets RCSB PDB PDBe
9FMB contains 17 α-helices and 76 β-strands across 4 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 | 297-302 | 6 | 1 |
| α-helix | 303-305 | 3 | |
| α-helix | 306-311 | 6 | |
| β-strand | 314-323 | 10 | 1 |
| β-strand | 330-335 | 6 | 2 |
| β-strand | 338 | 1 | 2 |
| β-strand | 344-346 | 3 | 1 |
| β-strand | 350-351 | 2 | 1 |
| β-strand | 357-366 | 10 | 1 |
| α-helix | 367-371 | 5 | |
| β-strand | 376-382 | 7 | 2 |
| β-strand | 385-392 | 8 | 2 |
| α-helix | 398 | 1 | |
| β-strand | 399 | 1 | 3 |
| α-helix | 400 | 1 | |
| β-strand | 403-410 | 8 | 4 |
| β-strand | 419-428 | 10 | 4 |
| β-strand | 429 | 1 | 3 |
| β-strand | 433-439 | 7 | 5 |
| β-strand | 443-444 | 2 | 5 |
| β-strand | 447-453 | 7 | 4 |
| β-strand | 463-471 | 9 | 4 |
| β-strand | 481-488 | 8 | 5 |
| β-strand | 493-500 | 8 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 297-302 | 6 | 6 |
| α-helix | 306-312 | 7 | |
| β-strand | 314-323 | 10 | 6 |
| α-helix | 326-328 | 3 | |
| β-strand | 330-335 | 6 | 7 |
| β-strand | 338 | 1 | 7 |
| β-strand | 344-346 | 3 | 6 |
| β-strand | 350-351 | 2 | 6 |
| β-strand | 357-366 | 10 | 6 |
| α-helix | 367-372 | 6 | |
| β-strand | 376-381 | 6 | 7 |
| β-strand | 388-392 | 5 | 7 |
| α-helix | 399-401 | 3 | |
| β-strand | 404-410 | 7 | 4 |
| β-strand | 419-428 | 10 | 4 |
| β-strand | 433-439 | 7 | 8 |
| β-strand | 442-444 | 3 | 8 |
| β-strand | 447-453 | 7 | 4 |
| β-strand | 463-471 | 9 | 4 |
| β-strand | 482-488 | 7 | 8 |
| β-strand | 493-496 | 4 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 297-302 | 6 | 9 |
| α-helix | 303-305 | 3 | |
| α-helix | 306-310 | 5 | |
| β-strand | 314-323 | 10 | 9 |
| β-strand | 330-335 | 6 | 10 |
| β-strand | 338 | 1 | 10 |
| α-helix | 339-340 | 2 | |
| β-strand | 344-346 | 3 | 9 |
| β-strand | 350-351 | 2 | 9 |
| β-strand | 357-366 | 10 | 9 |
| α-helix | 367-371 | 5 | |
| β-strand | 376-381 | 6 | 10 |
| β-strand | 388-392 | 5 | 10 |
| β-strand | 399 | 1 | 11 |
| α-helix | 400-401 | 2 | |
| β-strand | 403-406 | 4 | 12 |
| β-strand | 418-428 | 11 | 12 |
| β-strand | 429 | 1 | 11 |
| β-strand | 433-439 | 7 | 13 |
| β-strand | 442-444 | 3 | 13 |
| β-strand | 447 | 1 | 12 |
| β-strand | 450-453 | 4 | 12 |
| β-strand | 463-472 | 10 | 12 |
| β-strand | 481-488 | 8 | 13 |
| β-strand | 493-495 | 3 | 13 |
| β-strand | 498-500 | 3 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 297-302 | 6 | 14 |
| α-helix | 303-305 | 3 | |
| α-helix | 306-312 | 7 | |
| β-strand | 314-323 | 10 | 14 |
| β-strand | 330-335 | 6 | 15 |
| β-strand | 338 | 1 | 15 |
| β-strand | 344-346 | 3 | 14 |
| β-strand | 350-351 | 2 | 14 |
| β-strand | 357-366 | 10 | 14 |
| α-helix | 367-372 | 6 | |
| β-strand | 376-381 | 6 | 15 |
| β-strand | 388-392 | 5 | 15 |
| β-strand | 399 | 1 | 16 |
| β-strand | 404-412 | 9 | 17 |
| β-strand | 418-428 | 11 | 17 |
| β-strand | 429 | 1 | 16 |
| β-strand | 433-439 | 7 | 18 |
| β-strand | 442-444 | 3 | 18 |
| β-strand | 447-450 | 4 | 17 |
| β-strand | 463-471 | 9 | 17 |
| β-strand | 482-488 | 7 | 18 |
| β-strand | 493-498 | 6 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform 1 of Immunoglobulin heavy constant delta | A, B, C, D | protein | 234 | Homo sapiens | P01880 (AlphaFold model) |
>9FMB_1 Isoform 1 of Immunoglobulin heavy constant delta (chains A, B, C, D) KTPECPSHTQPLGVYLLTPAVQDLWLRDKATFTCFVVGSDLKDAHLTWEVAGKVPTGGVE EGLLERHSNGSQSQHSRLTLPRSLWNAGTSVTCTLNHPSLPPQRLMALREPAAQAPVKLS LNLLASSDPPEAASWLLCEVSGFSPPNILLMWLEDQREVNTSGFAPARPPPQPRSTTFWA WSVLRVPAPPSPQPATYTCVVSHEDSRTLLNASRSLEVSYVTDHGPMKHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (EDO, ACT, PEG) are not listed.
The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes. Davies, A.M., Bui, T.T.T., Pacheco-Gomez, R. et al. Proteins (2025) 93:786-800. DOI 10.1002/prot.26771 · PubMed
Other PDB entries of the same protein (UniProt P01880 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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