2.2A resolution structure of Proteasome Assembly Chaperone Hsm3. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Apr 2013.
Explore 4FP7 in 3D Show helices and sheets RCSB PDB PDBe
4FP7 contains 78 α-helices and 0 β-strands across 2 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 | 21-31 | 11 | |
| α-helix | 40-53 | 14 | |
| α-helix | 63-74 | 12 | |
| α-helix | 84-94 | 11 | |
| α-helix | 100-106 | 7 | |
| α-helix | 109-116 | 8 | |
| α-helix | 121-132 | 12 | |
| α-helix | 137-142 | 6 | |
| α-helix | 145-153 | 9 | |
| α-helix | 161-174 | 14 | |
| α-helix | 178-182 | 5 | |
| α-helix | 183-187 | 5 | |
| 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 | 275-283 | 9 | |
| α-helix | 289-306 | 18 | |
| α-helix | 315-320 | 6 | |
| α-helix | 321-325 | 5 | |
| α-helix | 331-333 | 3 | |
| α-helix | 334-340 | 7 | |
| α-helix | 343-349 | 7 | |
| α-helix | 351-357 | 7 | |
| α-helix | 365-371 | 7 | |
| α-helix | 375-381 | 7 | |
| α-helix | 382-384 | 3 | |
| α-helix | 387-391 | 5 | |
| α-helix | 395-405 | 11 | |
| α-helix | 409-418 | 10 | |
| α-helix | 420-427 | 8 | |
| α-helix | 432-434 | 3 | |
| α-helix | 438-452 | 15 | |
| α-helix | 456-459 | 4 | |
| α-helix | 460-462 | 3 | |
| α-helix | 463-475 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-53 | 12 | |
| α-helix | 63-73 | 11 | |
| α-helix | 84-94 | 11 | |
| α-helix | 95-97 | 3 | |
| α-helix | 100-106 | 7 | |
| α-helix | 109-117 | 9 | |
| α-helix | 121-132 | 12 | |
| α-helix | 139-142 | 4 | |
| α-helix | 145-153 | 9 | |
| α-helix | 161-174 | 14 | |
| α-helix | 178-185 | 8 | |
| α-helix | 189-198 | 10 | |
| α-helix | 201-214 | 14 | |
| α-helix | 215-217 | 3 | |
| α-helix | 220-222 | 3 | |
| 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 | 275-283 | 9 | |
| α-helix | 289-306 | 18 | |
| α-helix | 315-320 | 6 | |
| α-helix | 321-325 | 5 | |
| α-helix | 331-333 | 3 | |
| α-helix | 334-340 | 7 | |
| α-helix | 343-357 | 15 | |
| α-helix | 365-371 | 7 | |
| α-helix | 375-379 | 5 | |
| α-helix | 382-384 | 3 | |
| α-helix | 387-391 | 5 | |
| α-helix | 395-405 | 11 | |
| α-helix | 409-418 | 10 | |
| α-helix | 420-427 | 8 | |
| α-helix | 438-452 | 15 | |
| α-helix | 455-459 | 5 | |
| α-helix | 460-462 | 3 | |
| α-helix | 463-475 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA mismatch repair protein HSM3 | A, B | protein | 491 | Saccharomyces cerevisiae | P38348 (AlphaFold model) |
>4FP7_1 DNA mismatch repair protein HSM3 (chains A, B) GPLTRRASVGSMSEKETNYVENLLTQLENELNEDNLPEDINTLLRKCSLNLVTVVSLPDM DVKPLLATIKRFLTSNVSYDSLNYDYLLDVVDKLVPMADFDDVLEVYSAEDLVKALRSEI DPLKVAACRVIENSQPKGLFATSNIIDILLDILFDEKVENDKLITAIEKALERLSTDELI RRRLFDNNLPYLVSVKGRMETVSFVRLIDFLTIEFQFISGPEFKDIIFCFTKEEILKSVE DILVFIELVNYYTKFLLEIRNQDKYWALRHVKKILPVFAQLFEDTENYPDVRAFSTNCLL QLFAEVSRIEEDEYSLFKTMDKDSLKIGSEAKLITEWLELINPQYLVKYHKDVVENYFHV SGYSIGMLRNLSADEECFNAIRNKFSAEIVLRLPYLEQMQVVETLTRYEYTSKFLLNEMP KVMGSLIGDGSAGAIIDLETVHYRNSALRNLLDKGEEKLSVWYEPLLREYSKAVNGKNYS TGSETKIADCR
2.2A resolution structure of Proteasome Assembly Chaperone Hsm3. Singh, R., Lovell, S., Zolkiewski, M. et al. To be published.
Other PDB entries of the same protein (UniProt P38348 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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