Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, quadruple mutant, I222 form. Determined by X-ray diffraction at 4.19 Å resolution. Released 20 May 2015.
Explore 4QES in 3D Show helices and sheets RCSB PDB PDBe
4QES contains 77 α-helices and 39 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 | 25-29 | 5 | 2 |
| α-helix | 30-31 | 2 | |
| α-helix | 36-39 | 4 | |
| α-helix | 40-48 | 9 | |
| β-strand | 52-56 | 5 | 2 |
| α-helix | 57-58 | 2 | |
| α-helix | 73-87 | 15 | |
| β-strand | 92-97 | 6 | 2 |
| α-helix | 100-111 | 12 | |
| β-strand | 116-122 | 7 | 2 |
| β-strand | 130 | 1 | 3 |
| β-strand | 140 | 1 | 3 |
| α-helix | 142-154 | 13 | |
| α-helix | 157-168 | 12 | |
| α-helix | 170-173 | 4 | |
| β-strand | 174 | 1 | 4 |
| β-strand | 178 | 1 | 4 |
| α-helix | 180-191 | 12 | |
| α-helix | 195-204 | 10 | |
| α-helix | 213-215 | 3 | |
| β-strand | 220-225 | 6 | 2 |
| α-helix | 233-243 | 11 | |
| β-strand | 248-252 | 5 | 2 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-295 | 32 | |
| α-helix | 299 | 1 | |
| α-helix | 302-315 | 14 | |
| α-helix | 322-330 | 9 | |
| α-helix | 337-350 | 14 | |
| α-helix | 357-360 | 4 | |
| α-helix | 361-366 | 6 | |
| α-helix | 369-371 | 3 | |
| α-helix | 373-386 | 14 | |
| α-helix | 392-399 | 8 | |
| α-helix | 404-415 | 12 | |
| α-helix | 423-440 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-8 | 7 | 5 |
| β-strand | 11-16 | 6 | 5 |
| β-strand | 17-20 | 4 | 6 |
| β-strand | 25-29 | 5 | 6 |
| α-helix | 36-39 | 4 | |
| α-helix | 40-48 | 9 | |
| β-strand | 52-56 | 5 | 6 |
| α-helix | 57-58 | 2 | |
| α-helix | 73-87 | 15 | |
| β-strand | 92-97 | 6 | 6 |
| α-helix | 100-111 | 12 | |
| β-strand | 116-122 | 7 | 6 |
| β-strand | 130 | 1 | 7 |
| β-strand | 140 | 1 | 7 |
| α-helix | 142-154 | 13 | |
| α-helix | 157-168 | 12 | |
| α-helix | 170-173 | 4 | |
| β-strand | 174 | 1 | 8 |
| β-strand | 178 | 1 | 8 |
| α-helix | 180-191 | 12 | |
| α-helix | 195-204 | 10 | |
| α-helix | 213-215 | 3 | |
| β-strand | 220-225 | 6 | 6 |
| α-helix | 233-243 | 11 | |
| β-strand | 248-252 | 5 | 6 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-295 | 32 | |
| α-helix | 299 | 1 | |
| α-helix | 302-315 | 14 | |
| α-helix | 322-330 | 9 | |
| α-helix | 337-350 | 14 | |
| α-helix | 357-360 | 4 | |
| α-helix | 361-366 | 6 | |
| α-helix | 369-371 | 3 | |
| α-helix | 373-387 | 15 | |
| α-helix | 392-399 | 8 | |
| α-helix | 404-415 | 12 | |
| α-helix | 423-440 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-8 | 7 | 9 |
| β-strand | 11-16 | 6 | 9 |
| β-strand | 17-20 | 4 | 10 |
| β-strand | 25-29 | 5 | 10 |
| α-helix | 30-31 | 2 | |
| α-helix | 36-39 | 4 | |
| α-helix | 40-48 | 9 | |
| β-strand | 52-56 | 5 | 10 |
| α-helix | 57-58 | 2 | |
| α-helix | 73-87 | 15 | |
| β-strand | 92-97 | 6 | 10 |
| α-helix | 100-111 | 12 | |
| β-strand | 116-122 | 7 | 10 |
| β-strand | 130 | 1 | 11 |
| β-strand | 140 | 1 | 11 |
| α-helix | 142-154 | 13 | |
| α-helix | 157-168 | 12 | |
| α-helix | 170-173 | 4 | |
| β-strand | 174 | 1 | 12 |
| β-strand | 178 | 1 | 12 |
| α-helix | 180-191 | 12 | |
| α-helix | 195-204 | 10 | |
| α-helix | 213-215 | 3 | |
| β-strand | 220-225 | 6 | 10 |
| α-helix | 237-243 | 7 | |
| β-strand | 248-252 | 5 | 10 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-295 | 32 | |
| α-helix | 299 | 1 | |
| α-helix | 302-315 | 14 | |
| α-helix | 322-330 | 9 | |
| α-helix | 337-350 | 14 | |
| α-helix | 357-360 | 4 | |
| α-helix | 361-366 | 6 | |
| α-helix | 369-371 | 3 | |
| α-helix | 373-387 | 15 | |
| α-helix | 392-399 | 8 | |
| α-helix | 404-415 | 12 | |
| α-helix | 423-440 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Non-haem bromoperoxidase BPO-A2, Matrix protein 1 chimera | A, B, C | protein | 456 | Streptomyces aureofaciens, Influenza A virus | P03485 (AlphaFold model), P29715 (AlphaFold model) |
>4QES_1 Non-haem bromoperoxidase BPO-A2, Matrix protein 1 chimera (chains A, B, C) MPFITVGQENSTSIDLYYEDHGTGTPVVLIHGFPLSGHSWERQSAALLDAGARVITYDRR GFGQSSQPTTGYDYDTFAADLNTVLETLDLQDAVLVGFSMGTGEVARYVSSYGTARIAAV AFLASLEPFLLKTDDNPDGAAPQEFFDGIVAAVKADRYAFYTGFFNDFYNLDENLGTRIS EEAVRNSWNTAASGGFFAAAAAPTTWYTDFRADIPRIDVPALILHGTGDRTLPIENTARV FHKALPSAEYVEVEGAPHGLLWTHAEEVNTALLAFLAKAQEAQKQKLLTEVETYVLSIIP SGPLKAEIAQRLEDVFAGKNTDLEVLMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQR RRFVQNALNGNGDPNNMDKAVKLYRKLKREITFHGAKEISLSYSAGALASCMGLIYNRMG AVTTEVAFGLVCATCEQIADSQHRSHRQLEHHHHHH
Structural transition of a protein nanocage as a function of pH and salt concentration. Lai, Y.-T., Yeates, T.O. To be published.
Other PDB entries of the same protein (UniProt P03485 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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