yeast regulatory particle proteasome assembly chaperone Hsm3. Determined by X-ray diffraction at 2.1 Å resolution. Released 11 Apr 2012.
Explore 4A3T in 3D Show helices and sheets RCSB PDB PDBe
4A3T contains 80 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 | 9-19 | 11 | |
| α-helix | 29-41 | 13 | |
| α-helix | 52-63 | 12 | |
| α-helix | 73-86 | 14 | |
| α-helix | 89-95 | 7 | |
| α-helix | 98-105 | 8 | |
| α-helix | 110-121 | 12 | |
| α-helix | 134-142 | 9 | |
| α-helix | 150-163 | 14 | |
| α-helix | 167-171 | 5 | |
| α-helix | 172-176 | 5 | |
| α-helix | 178-187 | 10 | |
| α-helix | 190-204 | 15 | |
| α-helix | 209-211 | 3 | |
| α-helix | 214-217 | 4 | |
| α-helix | 221-228 | 8 | |
| α-helix | 231-250 | 20 | |
| α-helix | 254-256 | 3 | |
| α-helix | 257-260 | 4 | |
| α-helix | 261-263 | 3 | |
| α-helix | 264-272 | 9 | |
| α-helix | 278-295 | 18 | |
| α-helix | 300-309 | 10 | |
| α-helix | 310-314 | 5 | |
| α-helix | 320-322 | 3 | |
| α-helix | 323-329 | 7 | |
| α-helix | 332-338 | 7 | |
| α-helix | 340-346 | 7 | |
| α-helix | 354-360 | 7 | |
| α-helix | 364-368 | 5 | |
| α-helix | 371-373 | 3 | |
| α-helix | 376-381 | 6 | |
| α-helix | 384-395 | 12 | |
| α-helix | 398-407 | 10 | |
| α-helix | 409-416 | 8 | |
| α-helix | 427-441 | 15 | |
| α-helix | 445-448 | 4 | |
| α-helix | 449-451 | 3 | |
| α-helix | 452-464 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-20 | 13 | |
| α-helix | 29-40 | 12 | |
| α-helix | 52-63 | 12 | |
| α-helix | 66-68 | 3 | |
| α-helix | 73-86 | 14 | |
| α-helix | 89-95 | 7 | |
| α-helix | 98-106 | 9 | |
| α-helix | 110-121 | 12 | |
| α-helix | 134-142 | 9 | |
| α-helix | 150-163 | 14 | |
| α-helix | 167-171 | 5 | |
| α-helix | 172-176 | 5 | |
| α-helix | 178-187 | 10 | |
| α-helix | 190-204 | 15 | |
| α-helix | 209-211 | 3 | |
| α-helix | 214-217 | 4 | |
| α-helix | 221-228 | 8 | |
| α-helix | 231-250 | 20 | |
| α-helix | 254-256 | 3 | |
| α-helix | 257-260 | 4 | |
| α-helix | 261-263 | 3 | |
| α-helix | 264-272 | 9 | |
| α-helix | 278-295 | 18 | |
| α-helix | 304-309 | 6 | |
| α-helix | 310-314 | 5 | |
| α-helix | 320-322 | 3 | |
| α-helix | 323-329 | 7 | |
| α-helix | 332-338 | 7 | |
| α-helix | 340-346 | 7 | |
| α-helix | 354-360 | 7 | |
| α-helix | 364-368 | 5 | |
| α-helix | 371-373 | 3 | |
| α-helix | 376-381 | 6 | |
| α-helix | 384-395 | 12 | |
| α-helix | 398-407 | 10 | |
| α-helix | 409-416 | 8 | |
| α-helix | 421-423 | 3 | |
| α-helix | 427-441 | 15 | |
| α-helix | 445-448 | 4 | |
| α-helix | 449-451 | 3 | |
| α-helix | 452-464 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA mismatch repair protein HSM3 | A, B | protein | 485 | SACCHAROMYCES CEREVISIAE | P38348 (AlphaFold model) |
>4A3T_1 DNA MISMATCH REPAIR PROTEIN HSM3 (chains A, B) GAMADPSEKETNYVENLLTQLENELNEDNLPEDINTLLRKCSLNLVTVVSLPDMDVKPLL ATIKRFLTSNVSYDSLNYDYLLDVVDKLVPMADFDDVLEVYSAEDLVKALRSEIDPLKVA ACRVIENSQPKGLFATSNIIDILLDILFDEKVENDKLITAIEKALERLSTDELIRRRLFD NNLPYLVSVKGRMETVSFVRLIDFLTIEFQFISGPEFKDIIFCFTKEEILKSVEDILVFI ELVNYYTKFLLEIRNQDKYWALRHVKKILPVFAQLFEDTENYPDVRAFSTNCLLQLFAEV SRIEEDEYSLFKTMDKDSLKIGSEAKLITEWLELINPQYLVKYHKDVVENYFHVSGYSIG MLRNLSADEECFNAIRNKFSAEIVLRLPYLEQMQVVETLTRYEYTSKFLLNEMPKVMGSL IGDGSAGAIIDLETVHYRNSALRNLLDKGEEKLSVWYEPLLREYSKAVNGKNYSTGSETK IADCR
Dual Functions of the Hsm3 Protein in Chaperoning and Scaffolding Regulatory Particle Subunits During the Proteasome Assembly. Barrault, M.B., Richet, N., Godard, C. et al. Proc Natl Acad Sci U S A (2012) 109:E1001. DOI 10.1073/PNAS.1116538109 · 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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