Crystal structure of yeast proteasome interacting protein. Determined by X-ray diffraction at 2.05 Å resolution. Released 22 Feb 2012.
Explore 3VLD in 3D Show helices and sheets RCSB PDB PDBe
3VLD contains 82 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 | 10-21 | 12 | |
| α-helix | 25-26 | 2 | |
| α-helix | 29-42 | 14 | |
| 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 | 126-129 | 4 | |
| 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 | 214-217 | 4 | |
| α-helix | 221-227 | 7 | |
| 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 | 278-283 | 6 | |
| α-helix | 285-295 | 11 | |
| 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 | 351-353 | 3 | |
| α-helix | 354-360 | 7 | |
| α-helix | 364-368 | 5 | |
| α-helix | 371-373 | 3 | |
| α-helix | 376-380 | 5 | |
| α-helix | 384-394 | 11 | |
| 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-21 | 11 | |
| α-helix | 29-42 | 14 | |
| α-helix | 52-62 | 11 | |
| α-helix | 73-86 | 14 | |
| α-helix | 89-95 | 7 | |
| α-helix | 98-106 | 9 | |
| α-helix | 110-121 | 12 | |
| α-helix | 128-131 | 4 | |
| 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 | 221-227 | 7 | |
| α-helix | 231-251 | 21 | |
| 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 | 320-329 | 10 | |
| 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 | 376-380 | 5 | |
| α-helix | 384-394 | 11 | |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA mismatch repair protein HSM3 | A, B | protein | 500 | Saccharomyces cerevisiae | P38348 (AlphaFold model) |
>3VLD_1 DNA mismatch repair protein HSM3 (chains A, B) MGSSHHHHHHSSGLVPRGSHMSEKETNYVENLLTQLENELNEDNLPEDINTLLRKCSLNL VTVVSLPDMDVKPLLATIKRFLTSNVSYDSLNYDYLLDVVDKLVPMADFDDVLEVYSAED LVKALRSEIDPLKVAACRVIENSQPKGLFATSNIIDILLDILFDEKVENDKLITAIEKAL ERLSTDELIRRRLFDNNLPYLVSVKGRMETVSFVRLIDFLTIEFQFISGPEFKDIIFCFT KEEILKSVEDILVFIELVNYYTKFLLEIRNQDKYWALRHVKKILPVFAQLFEDTENYPDV RAFSTNCLLQLFAEVSRIEEDEYSLFKTMDKDSLKIGSEAKLITEWLELINPQYLVKYHK DVVENYFHVSGYSIGMLRNLSADEECFNAIRNKFSAEIVLRLPYLEQMQVVETLTRYEYT SKFLLNEMPKVMGSLIGDGSAGAIIDLETVHYRNSALRNLLDKGEEKLSVWYEPLLREYS KAVNGKNYSTGSETKIADCR
Structural basis for specific recognition of Rpt1, an ATPase subunit of the 26S proteasome, by a proteasome-dedicated chaperone Hsm3. Takagi, K., Kim, S., Yukii, H. et al. J Biol Chem (2012) 287:12172-12182. DOI 10.1074/jbc.M112.345876 · 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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