Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains. Determined by X-ray diffraction at 3.0 Å resolution. Released 20 Jun 2012.
Explore 3VDX in 3D Show helices and sheets RCSB PDB PDBe
3VDX contains 73 α-helices and 43 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 |
|---|---|---|---|
| β-strand | 2-8 | 7 | 1 |
| β-strand | 11-16 | 6 | 1 |
| β-strand | 17-20 | 4 | 2 |
| β-strand | 24-29 | 6 | 2 |
| α-helix | 36-39 | 4 | |
| α-helix | 42-49 | 8 | |
| β-strand | 51-56 | 6 | 2 |
| α-helix | 57-58 | 2 | |
| α-helix | 73-87 | 15 | |
| β-strand | 92-97 | 6 | 2 |
| α-helix | 98-101 | 4 | |
| α-helix | 102-111 | 10 | |
| β-strand | 116-122 | 7 | 2 |
| β-strand | 130 | 1 | 3 |
| β-strand | 140 | 1 | 3 |
| α-helix | 142-154 | 13 | |
| α-helix | 156-167 | 12 | |
| β-strand | 174 | 1 | 4 |
| β-strand | 178 | 1 | 4 |
| α-helix | 180-191 | 12 | |
| α-helix | 197-200 | 4 | |
| α-helix | 201-204 | 4 | |
| β-strand | 221-225 | 5 | 2 |
| α-helix | 233-235 | 3 | |
| α-helix | 237-243 | 7 | |
| β-strand | 248-252 | 5 | 2 |
| α-helix | 264-294 | 31 | |
| α-helix | 303-315 | 13 | |
| α-helix | 322-330 | 9 | |
| α-helix | 337-350 | 14 | |
| α-helix | 362-368 | 7 | |
| α-helix | 369-371 | 3 | |
| α-helix | 379-386 | 8 | |
| α-helix | 392-399 | 8 | |
| α-helix | 404-416 | 13 | |
| α-helix | 423-436 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 5 |
| β-strand | 8 | 1 | 6 |
| β-strand | 11 | 1 | 6 |
| β-strand | 14-16 | 3 | 5 |
| β-strand | 17-21 | 5 | 7 |
| β-strand | 25-29 | 5 | 7 |
| α-helix | 36-39 | 4 | |
| α-helix | 40-49 | 10 | |
| β-strand | 52-56 | 5 | 7 |
| α-helix | 57-58 | 2 | |
| α-helix | 73-86 | 14 | |
| β-strand | 92-97 | 6 | 7 |
| α-helix | 98-100 | 3 | |
| α-helix | 101-107 | 7 | |
| β-strand | 116-122 | 7 | 7 |
| β-strand | 130 | 1 | 8 |
| β-strand | 140 | 1 | 8 |
| α-helix | 142-154 | 13 | |
| α-helix | 156-167 | 12 | |
| β-strand | 174 | 1 | 9 |
| β-strand | 178 | 1 | 9 |
| α-helix | 180-191 | 12 | |
| α-helix | 202-204 | 3 | |
| β-strand | 221-225 | 5 | 7 |
| α-helix | 233-235 | 3 | |
| α-helix | 237-243 | 7 | |
| β-strand | 248-252 | 5 | 7 |
| α-helix | 264-283 | 20 | |
| α-helix | 287-297 | 11 | |
| α-helix | 303-315 | 13 | |
| α-helix | 322-328 | 7 | |
| α-helix | 337-350 | 14 | |
| α-helix | 362-366 | 5 | |
| α-helix | 373-377 | 5 | |
| α-helix | 379-386 | 8 | |
| α-helix | 392-396 | 5 | |
| α-helix | 404-413 | 10 | |
| α-helix | 424-433 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 10 |
| β-strand | 8 | 1 | 11 |
| β-strand | 11 | 1 | 11 |
| β-strand | 14-16 | 3 | 10 |
| β-strand | 17-20 | 4 | 12 |
| β-strand | 25-29 | 5 | 12 |
| α-helix | 36-39 | 4 | |
| α-helix | 42-49 | 8 | |
| β-strand | 52-56 | 5 | 12 |
| α-helix | 57-58 | 2 | |
| α-helix | 73-87 | 15 | |
| β-strand | 92-97 | 6 | 12 |
| α-helix | 100-111 | 12 | |
| β-strand | 116-122 | 7 | 12 |
| β-strand | 130 | 1 | 13 |
| β-strand | 140 | 1 | 13 |
| α-helix | 142-154 | 13 | |
| α-helix | 156-163 | 8 | |
| α-helix | 165-168 | 4 | |
| α-helix | 170-173 | 4 | |
| β-strand | 174 | 1 | 14 |
| β-strand | 178 | 1 | 14 |
| α-helix | 180-191 | 12 | |
| α-helix | 195-200 | 6 | |
| α-helix | 201-204 | 4 | |
| α-helix | 213-215 | 3 | |
| β-strand | 220-225 | 6 | 12 |
| α-helix | 233-235 | 3 | |
| α-helix | 237-243 | 7 | |
| β-strand | 248-252 | 5 | 12 |
| α-helix | 264-278 | 15 | |
| α-helix | 280-283 | 4 | |
| α-helix | 285-295 | 11 | |
| α-helix | 299 | 1 | |
| α-helix | 302-316 | 15 | |
| α-helix | 322-330 | 9 | |
| α-helix | 337-349 | 13 | |
| α-helix | 361-364 | 4 | |
| α-helix | 373-386 | 14 | |
| α-helix | 392-398 | 7 | |
| α-helix | 404-415 | 12 | |
| α-helix | 423-436 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Designed 16nm tetrahedral protein cage containing Non-haem bromoperoxidase BPO-A2 and Matrix… | A, B, C | protein | 456 | Streptomyces aureofaciens, Influenza A virus | P03485 (AlphaFold model), P29715 (AlphaFold model) |
>3VDX_1 Designed 16nm tetrahedral protein cage containing Non-haem bromoperoxidase BPO-A2 and Matrix protein 1 (chains A, B, C) MPFITVGQENSTSIDLYYEDHGTGVPVVLIHGFPLSGHSWERQSAALLDAGYRVITYDRR GFGQSSQPTTGYDYDTFAADLNTVLETLDLQDAVLVGFSMGTGEVARYVSSYGTARIAAV AFLASLEPFLLKTDDNPDGAAPQEFFDGIVAAVKADRYAFYTGFFNDFYNLDENLGTRIS EEAVRNSWNTAASGGFFAAAAAPTTWYTDFRADIPRIDVPALILHGTGDRTLPIENTARV FHKALPSAEYVEVEGAPHGLLWTHAEEVNTALLAFLAKALEAQKQKLLTEVETYVLSIIP SGPLKAEIAQRLEDVFAGKNTDLEVLMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQR RRFVQNALNGNGDPNNMDKAVKLYRKLKREITFHGAKEISLSYSAGALASCMGLIYNRMG AVTTEVAFGLVCATCEQIADSQHRSHRQLEHHHHHH
Structure of a 16-nm cage designed by using protein oligomers. Lai, Y.T., Cascio, D., Yeates, T.O. Science (2012) 336:1129-1129. DOI 10.1126/science.1219351 · PubMed
Other PDB entries of the same protein (UniProt P03485 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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