Crystal structure of yeast Rpn14. Determined by X-ray diffraction at 1.6 Å resolution. Released 2 May 2012.
Explore 3VL1 in 3D Show helices and sheets RCSB PDB PDBe
3VL1 contains 13 α-helices and 80 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 |
|---|---|---|---|
| β-strand | 3-5 | 3 | 1 |
| α-helix | 6-7 | 2 | |
| β-strand | 8-10 | 3 | 2 |
| α-helix | 14-19 | 6 | |
| β-strand | 27-35 | 9 | 2 |
| β-strand | 38-45 | 8 | 2 |
| β-strand | 54 | 1 | 2 |
| β-strand | 60-65 | 6 | 3 |
| β-strand | 68-73 | 6 | 3 |
| β-strand | 76-81 | 6 | 3 |
| β-strand | 85-86 | 2 | 4 |
| α-helix | 92 | 1 | |
| β-strand | 96-102 | 7 | 5 |
| β-strand | 108-113 | 6 | 5 |
| β-strand | 118-121 | 4 | 5 |
| β-strand | 127-131 | 5 | 5 |
| β-strand | 139-144 | 6 | 6 |
| β-strand | 150-155 | 6 | 6 |
| β-strand | 159-164 | 6 | 6 |
| β-strand | 172-175 | 4 | 6 |
| β-strand | 181-187 | 7 | 7 |
| β-strand | 192-197 | 6 | 7 |
| β-strand | 202-206 | 5 | 7 |
| β-strand | 211-216 | 6 | 7 |
| β-strand | 218 | 1 | 8 |
| β-strand | 221 | 1 | 8 |
| β-strand | 226-233 | 8 | 9 |
| α-helix | 234-235 | 2 | |
| α-helix | 240-242 | 3 | |
| α-helix | 245-248 | 4 | |
| β-strand | 257-263 | 7 | 9 |
| β-strand | 268-272 | 5 | 9 |
| β-strand | 278-282 | 5 | 9 |
| β-strand | 290-295 | 6 | 1 |
| β-strand | 302-307 | 6 | 1 |
| β-strand | 311-316 | 6 | 1 |
| β-strand | 325-329 | 5 | 1 |
| β-strand | 335-341 | 7 | 3 |
| β-strand | 344-349 | 6 | 3 |
| β-strand | 353-358 | 6 | 3 |
| β-strand | 359-360 | 2 | 10 |
| β-strand | 369-370 | 2 | 10 |
| β-strand | 376-378 | 3 | 3 |
| α-helix | 383-385 | 3 | |
| β-strand | 387-391 | 5 | 4 |
| β-strand | 399-404 | 6 | 4 |
| β-strand | 408-413 | 6 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 11 |
| α-helix | 6 | 1 | |
| β-strand | 7-10 | 4 | 12 |
| α-helix | 14-19 | 6 | |
| β-strand | 27-35 | 9 | 12 |
| β-strand | 38-45 | 8 | 12 |
| β-strand | 54 | 1 | 12 |
| β-strand | 60-65 | 6 | 13 |
| β-strand | 68-73 | 6 | 13 |
| β-strand | 76-81 | 6 | 13 |
| β-strand | 85-86 | 2 | 14 |
| α-helix | 92-93 | 2 | |
| β-strand | 96-102 | 7 | 15 |
| β-strand | 108-113 | 6 | 15 |
| β-strand | 118-121 | 4 | 15 |
| β-strand | 127-131 | 5 | 15 |
| β-strand | 139-144 | 6 | 16 |
| β-strand | 150-155 | 6 | 16 |
| β-strand | 160-164 | 5 | 16 |
| β-strand | 172-174 | 3 | 16 |
| β-strand | 181-187 | 7 | 17 |
| β-strand | 192-197 | 6 | 17 |
| β-strand | 202-206 | 5 | 17 |
| β-strand | 211-216 | 6 | 17 |
| β-strand | 218 | 1 | 18 |
| β-strand | 221 | 1 | 18 |
| β-strand | 226-233 | 8 | 19 |
| α-helix | 240-242 | 3 | |
| α-helix | 245-248 | 4 | |
| β-strand | 257-263 | 7 | 19 |
| β-strand | 268-272 | 5 | 19 |
| β-strand | 278-282 | 5 | 19 |
| β-strand | 290-295 | 6 | 11 |
| β-strand | 302-307 | 6 | 11 |
| β-strand | 311-316 | 6 | 11 |
| β-strand | 325-329 | 5 | 11 |
| β-strand | 335-341 | 7 | 13 |
| β-strand | 344-349 | 6 | 13 |
| β-strand | 353-358 | 6 | 13 |
| β-strand | 359-360 | 2 | 20 |
| β-strand | 369-370 | 2 | 20 |
| β-strand | 376-378 | 3 | 13 |
| α-helix | 383-385 | 3 | |
| β-strand | 387-391 | 5 | 14 |
| β-strand | 399-404 | 6 | 14 |
| β-strand | 408-413 | 6 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 26S proteasome regulatory subunit RPN14 | A, B | protein | 420 | Saccharomyces cerevisiae | P53196 (AlphaFold model) |
>3VL1_1 26S proteasome regulatory subunit RPN14 (chains A, B) GSHMTKTITVAHIQYDFKAVLEENDENDDEFYINVDKNLNEIKEHKIVVLGNSRGVDAGK GNTFEKVGSHLYKARLDGHDFLFNTIIRDGSKMLKRADYTAVDTAKLQMRRFILGTTEGD IKVLDSNFNLQREIDQAHVSEITKLKFFPSGEALISSSQDMQLKIWSVKDGSNPRTLIGH RATVTDIAIIDRGRNVLSASLDGTIRLWECGTGTTIHTFNRKENPHDGVNSIALFVGTDR QLHEISTSKKNNLEFGTYGKYVIAGHVSGVITVHNVFSKEQTIQLPSKFTCSCNSLTVDG NNANYIYAGYENGMLAQWDLRSPECPVGEFLINEGTPINNVYFAAGALFVSSGFDTSIKL DIISDPESERPAIEFETPTFLVSNDDAVSQFCYVSDDESNGEVLEVGKNNFCALYNLSNP
New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 A resolution. Kim, S., Nishide, A., Saeki, Y. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2012) 68:517-521. DOI 10.1107/S1744309112011359 · PubMed
Other PDB entries of the same protein (UniProt P53196 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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