5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1. Determined by X-ray diffraction at 5.0 Å resolution. Released 10 Apr 2013.
Explore 4JPO in 3D Show helices and sheets RCSB PDB PDBe
4JPO contains 82 α-helices and 4 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 |
|---|---|---|---|
| α-helix | 24-31 | 8 | |
| α-helix | 40-50 | 11 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-73 | 10 | |
| α-helix | 84-97 | 14 | |
| α-helix | 100-106 | 7 | |
| α-helix | 109-117 | 9 | |
| α-helix | 121-132 | 12 | |
| α-helix | 145-153 | 9 | |
| α-helix | 161-174 | 14 | |
| α-helix | 178-184 | 7 | |
| α-helix | 189-198 | 10 | |
| α-helix | 201-215 | 15 | |
| α-helix | 225-228 | 4 | |
| α-helix | 232-238 | 7 | |
| α-helix | 242-261 | 20 | |
| α-helix | 265-267 | 3 | |
| α-helix | 268-271 | 4 | |
| α-helix | 272-274 | 3 | |
| α-helix | 276-283 | 8 | |
| α-helix | 291-294 | 4 | |
| α-helix | 296-308 | 13 | |
| α-helix | 316-320 | 5 | |
| α-helix | 321-325 | 5 | |
| α-helix | 331-333 | 3 | |
| α-helix | 334-340 | 7 | |
| α-helix | 343-355 | 13 | |
| α-helix | 365-371 | 7 | |
| α-helix | 375-379 | 5 | |
| α-helix | 387-391 | 5 | |
| α-helix | 395-405 | 11 | |
| α-helix | 409-413 | 5 | |
| α-helix | 414-418 | 5 | |
| α-helix | 420-427 | 8 | |
| α-helix | 440-452 | 13 | |
| α-helix | 456-459 | 4 | |
| α-helix | 463-474 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-31 | 8 | |
| α-helix | 47-50 | 4 | |
| α-helix | 51-53 | 3 | |
| α-helix | 64-73 | 10 | |
| α-helix | 85-94 | 10 | |
| α-helix | 103-106 | 4 | |
| α-helix | 109-117 | 9 | |
| α-helix | 121-132 | 12 | |
| α-helix | 145-153 | 9 | |
| α-helix | 161-174 | 14 | |
| α-helix | 178-184 | 7 | |
| α-helix | 189-198 | 10 | |
| α-helix | 203-215 | 13 | |
| α-helix | 225-228 | 4 | |
| α-helix | 232-238 | 7 | |
| α-helix | 242-261 | 20 | |
| α-helix | 265-267 | 3 | |
| α-helix | 268-271 | 4 | |
| α-helix | 272-274 | 3 | |
| α-helix | 276-283 | 8 | |
| α-helix | 291-294 | 4 | |
| α-helix | 296-308 | 13 | |
| α-helix | 316-320 | 5 | |
| α-helix | 321-325 | 5 | |
| α-helix | 331-333 | 3 | |
| α-helix | 334-340 | 7 | |
| α-helix | 343-355 | 13 | |
| α-helix | 366-371 | 6 | |
| α-helix | 375-379 | 5 | |
| α-helix | 387-391 | 5 | |
| α-helix | 395-405 | 11 | |
| α-helix | 409-413 | 5 | |
| α-helix | 414-418 | 5 | |
| α-helix | 420-427 | 8 | |
| α-helix | 439-452 | 14 | |
| α-helix | 456-459 | 4 | |
| α-helix | 463-471 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 384-395 | 12 | |
| β-strand | 398 | 1 | 1 |
| α-helix | 404-410 | 7 | |
| α-helix | 416-432 | 17 | |
| β-strand | 438 | 1 | 1 |
| α-helix | 440-449 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 384-395 | 12 | |
| β-strand | 398 | 1 | 2 |
| α-helix | 404-410 | 7 | |
| α-helix | 416-432 | 17 | |
| β-strand | 438 | 1 | 2 |
| α-helix | 440-450 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA mismatch repair protein HSM3 | A, B | protein | 491 | Saccharomyces cerevisiae | P38348 (AlphaFold model) |
| 26S protease regulatory subunit 7 homolog | C, D | protein | 100 | Saccharomyces cerevisiae | P33299 (AlphaFold model) |
>4JPO_1 DNA mismatch repair protein HSM3 (chains A, B) GPLTRRASVGSMSEKETNYVENLLTQLENELNEDNLPEDINTLLRKCSLNLVTVVSLPDM DVKPLLATIKRFLTSNVSYDSLNYDYLLDVVDKLVPMADFDDVLEVYSAEDLVKALRSEI DPLKVAACRVIENSQPKGLFATSNIIDILLDILFDEKVENDKLITAIEKALERLSTDELI RRRLFDNNLPYLVSVKGRMETVSFVRLIDFLTIEFQFISGPEFKDIIFCFTKEEILKSVE DILVFIELVNYYTKFLLEIRNQDKYWALRHVKKILPVFAQLFEDTENYPDVRAFSTNCLL QLFAEVSRIEEDEYSLFKTMDKDSLKIGSEAKLITEWLELINPQYLVKYHKDVVENYFHV SGYSIGMLRNLSADEECFNAIRNKFSAEIVLRLPYLEQMQVVETLTRYEYTSKFLLNEMP KVMGSLIGDGSAGAIIDLETVHYRNSALRNLLDKGEEKLSVWYEPLLREYSKAVNGKNYS TGSETKIADCR
>4JPO_2 26S protease regulatory subunit 7 homolog (chains C, D) MHHHHHHSQHMLPDLEGRANIFRIHSKSMSVERGIRWELISRLCPNSTGAELRSVCTEAG MFAIRARRKVATEKDFLKAVDKVISGYKKFSSTSRYMQYN
Reconfiguration of the proteasome during chaperone-mediated assembly. Park, S., Li, X., Kim, H.M. et al. Nature (2013) 497:512-516. DOI 10.1038/nature12123 · PubMed
Other PDB entries of the same protein (UniProt P38348 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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