FcMR binding at subunit Fcu3 of IgM pentamer. Determined by electron microscopy at 3.1 Å resolution. Released 12 Apr 2023.
Explore 8BPG in 3D Show helices and sheets RCSB PDB PDBe
8BPG contains 42 α-helices and 114 β-strands across 6 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 | 22 | 1 | 20 |
| β-strand | 32-38 | 7 | 21 |
| β-strand | 46-48 | 3 | 22 |
| β-strand | 50 | 1 | 23 |
| β-strand | 59 | 1 | 23 |
| β-strand | 63 | 1 | 22 |
| α-helix | 70-72 | 3 | |
| β-strand | 76-81 | 6 | 21 |
| β-strand | 86-92 | 7 | 21 |
| β-strand | 101 | 1 | 24 |
| β-strand | 104-106 | 3 | 22 |
| β-strand | 116 | 1 | 22 |
| β-strand | 117 | 1 | 20 |
| β-strand | 119 | 1 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 346-350 | 5 | 14 |
| α-helix | 351-353 | 3 | |
| α-helix | 354-360 | 7 | |
| β-strand | 366-370 | 5 | 14 |
| β-strand | 379-383 | 5 | 15 |
| α-helix | 396-399 | 4 | |
| β-strand | 400 | 1 | 16 |
| β-strand | 404 | 1 | 16 |
| β-strand | 407 | 1 | 14 |
| β-strand | 410 | 1 | 14 |
| α-helix | 415-419 | 5 | |
| β-strand | 424-429 | 6 | 15 |
| β-strand | 437 | 1 | 15 |
| β-strand | 440-441 | 2 | 15 |
| β-strand | 450 | 1 | 17 |
| β-strand | 453-457 | 5 | 18 |
| α-helix | 458-460 | 3 | |
| α-helix | 461-465 | 5 | |
| β-strand | 469-479 | 11 | 18 |
| β-strand | 480 | 1 | 17 |
| β-strand | 485-489 | 5 | 19 |
| β-strand | 494 | 1 | 19 |
| α-helix | 495-496 | 2 | |
| β-strand | 500-502 | 3 | 18 |
| β-strand | 506-507 | 2 | 18 |
| α-helix | 508 | 1 | |
| β-strand | 515-524 | 10 | 18 |
| α-helix | 525-529 | 5 | |
| β-strand | 534-539 | 6 | 19 |
| β-strand | 548-552 | 5 | 19 |
| α-helix | 558-560 | 3 | |
| β-strand | 567 | 1 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 346-350 | 5 | 6 |
| α-helix | 351-353 | 3 | |
| α-helix | 354-360 | 7 | |
| β-strand | 364-365 | 2 | 7 |
| β-strand | 366-370 | 5 | 6 |
| β-strand | 380-384 | 5 | 8 |
| β-strand | 389 | 1 | 8 |
| α-helix | 391-393 | 3 | |
| β-strand | 399-400 | 2 | 9 |
| β-strand | 404-405 | 2 | 9 |
| β-strand | 411-412 | 2 | 7 |
| α-helix | 415-420 | 6 | |
| β-strand | 424-428 | 5 | 8 |
| β-strand | 437-441 | 5 | 8 |
| β-strand | 450 | 1 | 10 |
| β-strand | 453-457 | 5 | 11 |
| α-helix | 458-460 | 3 | |
| α-helix | 463-465 | 3 | |
| β-strand | 470-479 | 10 | 11 |
| β-strand | 480 | 1 | 10 |
| β-strand | 485-490 | 6 | 12 |
| β-strand | 493-494 | 2 | 12 |
| α-helix | 495-496 | 2 | |
| α-helix | 497-499 | 3 | |
| β-strand | 500-502 | 3 | 11 |
| β-strand | 506-507 | 2 | 11 |
| α-helix | 508 | 1 | |
| β-strand | 515-523 | 9 | 11 |
| α-helix | 525-529 | 5 | |
| β-strand | 534-539 | 6 | 12 |
| β-strand | 549-552 | 4 | 12 |
| β-strand | 567 | 1 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fas apoptotic inhibitory molecule 3 | A, B | protein | 234 | Homo sapiens | O60667 (AlphaFold model) |
| Immunoglobulin heavy constant mu | C, D, E, F | protein | 348 | Homo sapiens | P01871 (AlphaFold model) |
>8BPG_1 Fas apoptotic inhibitory molecule 3 (chains A, B) RILPEVKVEGELGGSVTIKCPLPEMHVRIYLCREMAGSGTCGTVVSTTNFIKAEYKGRVT LKQYPRKNLFLVEVTQLTESDSGVYACGAGMNTDRGKTQKVTLNVHSEYEPSWEEQPMPE TPKWFHLPYLFQMPAYASSSKFVTRVTTPAQRGKVPPVHHSSPTTQITHRPRVSRASSVA GDKPRTFLPSTTASKISALEGLLKPQTPSYNHHTRLHRQRALDYGSQSGREGQG
>8BPG_2 Immunoglobulin heavy constant mu (chains C, D, E, F) IAELPPKVSVFVPPRDGFFGNPRKSKLICQATGFSPRQIQVSWLREGKQVGSGVTTDQVQ AEAKESGPTTYKVTSTLTIKESDWLGQSMFTCRVDHRGLTFQQNASSMCVPDQDTAIRVF AIPPSFASIFLTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAV GEASICEDDWNSGERFTCTVTHTDLPSPLKQTISRPKGVALHRPDVYLLPPAREQLNLRE SATITCLVTGFSPADVFVQWMQRGQPLSPEKYVTSAPMPEPQAPGRYFAHSILTVSEEEW NTGETYTCVVAHEALPNRVTERTVDKSTGKPTLYNVSLVMSDTAGTCY
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Structural basis for Fc receptor recognition of immunoglobulin M. Chen, Q., Menon, R.P., Masino, L. et al. Nat Struct Mol Biol (2023) 30:1033-1039. DOI 10.1038/s41594-023-00985-x · PubMed
Other PDB entries of the same protein (UniProt O60667 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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