Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation. Determined by X-ray diffraction at 2.6 Å resolution. Released 30 Sept 2008.
Explore 3DPL in 3D Show helices and sheets RCSB PDB PDBe
3DPL contains 25 α-helices and 21 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 | 405-416 | 12 | |
| β-strand | 417 | 1 | 1 |
| α-helix | 420-423 | 4 | |
| α-helix | 427-438 | 12 | |
| α-helix | 439-443 | 5 | |
| α-helix | 447-463 | 17 | |
| β-strand | 467 | 1 | 1 |
| α-helix | 470-482 | 13 | |
| α-helix | 487-513 | 27 | |
| α-helix | 523-525 | 3 | |
| β-strand | 526-532 | 7 | 2 |
| α-helix | 533-536 | 4 | |
| α-helix | 546-548 | 3 | |
| α-helix | 549-552 | 4 | |
| α-helix | 555-563 | 9 | |
| β-strand | 569-573 | 5 | 2 |
| α-helix | 575-577 | 3 | |
| β-strand | 579-585 | 7 | 2 |
| β-strand | 590-596 | 7 | 2 |
| α-helix | 597-603 | 7 | |
| α-helix | 604-606 | 3 | |
| β-strand | 614-615 | 2 | 3 |
| α-helix | 616-623 | 8 | |
| α-helix | 627-638 | 12 | |
| β-strand | 648-650 | 3 | 3 |
| α-helix | 657-659 | 3 | |
| β-strand | 665-668 | 4 | 3 |
| β-strand | 674-675 | 2 | 4 |
| β-strand | 680-681 | 2 | 4 |
| β-strand | 683-687 | 5 | 2 |
| α-helix | 697-723 | 27 | |
| β-strand | 728-729 | 2 | 5 |
| α-helix | 731-741 | 11 | |
| α-helix | 750-762 | 13 | |
| β-strand | 766-769 | 4 | 5 |
| β-strand | 772-778 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-35 | 14 | 2 |
| α-helix | 40-42 | 3 | |
| α-helix | 56-59 | 4 | |
| β-strand | 70-73 | 4 | 6 |
| β-strand | 78-80 | 3 | 6 |
| α-helix | 81-88 | 8 | |
| β-strand | 93 | 1 | 7 |
| β-strand | 100 | 1 | 7 |
| α-helix | 101 | 1 | |
| β-strand | 103-105 | 3 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cullin-5 | C | protein | 382 | Homo sapiens | Q93034 (AlphaFold model) |
| RING-box protein 1 | R | protein | 106 | Homo sapiens | P62877 (AlphaFold model) |
>3DPL_1 Cullin-5 (chains C) GSESKCPEELANYCDMLLRKTPLSKKLTSEEIEAKLKEVLKKLKYVQNKDVFMRYHKAHL TRRLILDISADSEIEENMVEWLREVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNK LALPADSVNIKILNAGAWSRSSEKVFVSLPTELEDLIPEVEEFYKKNHSGRKLHWHHLMS NGIITFKNEVGQYDLEVTTFQLAVLFAWNQRPREKISFENLKLATELPDAELRRTLWSLV AFPKLKRQVLLYEPQVNSPKDFTEGTLFSVNQEFSLIKNAKVQKRGKINLIGRLQLTTER MREEENEGIVQLRILRTQEAIIQIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQIE WLIEHKYIRRDESDINTFIYMA
>3DPL_2 RING-box protein 1 (chains R) GSMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQAS ATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Duda, D.M., Borg, L.A., Scott, D.C. et al. Cell (2008) 134:995-1006. DOI 10.1016/j.cell.2008.07.022 · PubMed
Other PDB entries of the same protein (UniProt Q93034 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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