System-wide modulation of HECT E3 ligases with selective ubiquitin variant probes: Rsp5 and UbV R5.4. Determined by X-ray diffraction at 2.31 Å resolution. Released 16 Mar 2016.
Explore 5HPL in 3D Show helices and sheets RCSB PDB PDBe
5HPL contains 61 α-helices and 44 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 | 435-443 | 9 | |
| α-helix | 446-448 | 3 | |
| α-helix | 450 | 1 | |
| β-strand | 451-459 | 9 | 1 |
| α-helix | 461-463 | 3 | |
| α-helix | 464-473 | 10 | |
| α-helix | 479-481 | 3 | |
| β-strand | 482-488 | 7 | 1 |
| α-helix | 496-511 | 16 | |
| α-helix | 514-516 | 3 | |
| β-strand | 519-521 | 3 | 2 |
| β-strand | 529-531 | 3 | 2 |
| α-helix | 535-537 | 3 | |
| α-helix | 541-557 | 17 | |
| β-strand | 566 | 1 | 2 |
| α-helix | 568-574 | 7 | |
| α-helix | 581-586 | 6 | |
| α-helix | 589-600 | 12 | |
| β-strand | 610 | 1 | 3 |
| β-strand | 612-617 | 6 | 4 |
| β-strand | 620-625 | 6 | 4 |
| α-helix | 630-632 | 3 | |
| β-strand | 634 | 1 | 3 |
| α-helix | 640-649 | 10 | |
| α-helix | 650-654 | 5 | |
| α-helix | 657-668 | 12 | |
| α-helix | 673-676 | 4 | |
| α-helix | 681-689 | 9 | |
| α-helix | 696-701 | 6 | |
| β-strand | 703-706 | 4 | 5 |
| α-helix | 713-724 | 12 | |
| α-helix | 727-738 | 12 | |
| α-helix | 742-744 | 3 | |
| α-helix | 748-750 | 3 | |
| β-strand | 752-753 | 2 | 6 |
| β-strand | 756-757 | 2 | 6 |
| β-strand | 760-763 | 4 | 5 |
| α-helix | 771-772 | 2 | |
| β-strand | 773-775 | 3 | 5 |
| β-strand | 780-782 | 3 | 5 |
| α-helix | 789-801 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 434-443 | 10 | |
| α-helix | 446-448 | 3 | |
| α-helix | 450 | 1 | |
| β-strand | 451-460 | 10 | 7 |
| α-helix | 461-463 | 3 | |
| α-helix | 464-473 | 10 | |
| β-strand | 482-489 | 8 | 7 |
| α-helix | 496-511 | 16 | |
| α-helix | 514-516 | 3 | |
| β-strand | 519-521 | 3 | 8 |
| β-strand | 529-531 | 3 | 8 |
| α-helix | 535-537 | 3 | |
| α-helix | 541-557 | 17 | |
| β-strand | 566 | 1 | 8 |
| α-helix | 568-574 | 7 | |
| α-helix | 581-583 | 3 | |
| α-helix | 584-587 | 4 | |
| α-helix | 589-600 | 12 | |
| β-strand | 610 | 1 | 9 |
| β-strand | 612-617 | 6 | 10 |
| β-strand | 620-625 | 6 | 10 |
| α-helix | 630-632 | 3 | |
| β-strand | 634 | 1 | 9 |
| α-helix | 640-652 | 13 | |
| α-helix | 654-656 | 3 | |
| α-helix | 657-668 | 12 | |
| α-helix | 673-676 | 4 | |
| α-helix | 681-689 | 9 | |
| α-helix | 696-701 | 6 | |
| β-strand | 703-706 | 4 | 11 |
| α-helix | 713-723 | 11 | |
| α-helix | 727-738 | 12 | |
| α-helix | 742-744 | 3 | |
| α-helix | 748-750 | 3 | |
| β-strand | 752-753 | 2 | 12 |
| β-strand | 756-757 | 2 | 12 |
| β-strand | 760-763 | 4 | 11 |
| α-helix | 771-772 | 2 | |
| β-strand | 773-775 | 3 | 11 |
| β-strand | 780-782 | 3 | 11 |
| α-helix | 789-801 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 13 |
| β-strand | 12-17 | 6 | 13 |
| β-strand | 22 | 1 | 14 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 13 |
| β-strand | 48-49 | 2 | 13 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 14 |
| α-helix | 57-59 | 3 | |
| β-strand | 65-71 | 7 | 13 |
| α-helix | 72-73 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 15 |
| β-strand | 12-17 | 6 | 15 |
| β-strand | 22 | 1 | 16 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 15 |
| β-strand | 48-49 | 2 | 15 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 16 |
| β-strand | 66-71 | 6 | 15 |
| α-helix | 72-73 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rsp5 | A, B | protein | 380 | Saccharomyces cerevisiae | P39940 (AlphaFold model) |
| Ubiquitin variant R5.4 | C, D | protein | 86 | Homo sapiens | P62987 (AlphaFold model) |
>5HPL_1 Rsp5 (chains A, B) QYKRDFRRKVIYFRSQPALRILPGQCHIKVRRKNIFEDAYQEIMRQTPEDLKKRLMIKFD GEEGLDYGGVSREFFFLLSHEMFNPFYCLFEYSAYDNYTIQINPNSGINPEHLNYFKFIG RVVGLGVFHRRFLDAFFVGALYKMMLRKKVVLQDMEGVDAEVYNSLNWMLENSIDGVLDL TFSADDERFGEVVTVDLKPDGRNIEVTDGNKKEYVELYTQWRIVDRVQEQFKAFMDGFNE LIPEDLVTVFDERELELLIGGIAEIDIEDWKKHTDYRGYQESDEVIQWFWKCVSEWDNEQ RARLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKAGEVQQLPKSHTCFNRVDLPQYVDY DSMKQKLTLAVEETIGFGQE
>5HPL_2 Ubiquitin variant R5.4 (chains C, D) MGHHHHHHMQIFVKTPTRKSISLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLED GRTLSDYNIQKESTLHLVLRLPGTIK
System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes. Zhang, W., Wu, K.P., Sartori, M.A. et al. Mol Cell (2016) 62:121-136. DOI 10.1016/j.molcel.2016.02.005 · PubMed
Other PDB entries of the same protein (UniProt P39940 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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