Structure of VHL-EloB-EloC-Cul2. Determined by X-ray diffraction at 3.2 Å resolution. Released 4 Mar 2015.
Explore 4WQO in 3D Show helices and sheets RCSB PDB PDBe
4WQO contains 28 α-helices and 29 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 |
|---|---|---|---|
| β-strand | 71-79 | 9 | 1 |
| α-helix | 83 | 1 | |
| β-strand | 84-89 | 6 | 2 |
| β-strand | 95-97 | 3 | 2 |
| β-strand | 101 | 1 | 2 |
| β-strand | 106-112 | 7 | 1 |
| β-strand | 116-121 | 6 | 2 |
| β-strand | 127 | 1 | 2 |
| β-strand | 129-130 | 2 | 1 |
| β-strand | 133 | 1 | 1 |
| β-strand | 136 | 1 | 2 |
| α-helix | 140-141 | 2 | |
| β-strand | 142 | 1 | 3 |
| β-strand | 145 | 1 | 3 |
| α-helix | 146 | 1 | |
| β-strand | 147-152 | 6 | 1 |
| α-helix | 158-169 | 12 | |
| α-helix | 172-177 | 6 | |
| α-helix | 183-189 | 7 | |
| α-helix | 194-206 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-8 | 7 | 4 |
| β-strand | 12-19 | 8 | 4 |
| β-strand | 23 | 1 | 5 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-45 | 4 | 4 |
| α-helix | 49 | 1 | |
| β-strand | 50 | 1 | 4 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 5 |
| β-strand | 68 | 1 | 6 |
| β-strand | 71 | 1 | 6 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 4 |
| β-strand | 80 | 1 | 7 |
| β-strand | 85 | 1 | 7 |
| α-helix | 86-88 | 3 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-103 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 4 |
| β-strand | 28-32 | 5 | 4 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 59-61 | 3 | 4 |
| α-helix | 67-83 | 17 | |
| α-helix | 89-92 | 4 | |
| α-helix | 97-99 | 3 | |
| α-helix | 100-110 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 8 |
| α-helix | 10-25 | 16 | |
| α-helix | 32-47 | 16 | |
| β-strand | 49 | 1 | 8 |
| α-helix | 54-77 | 24 | |
| α-helix | 85-104 | 20 | |
| α-helix | 106-107 | 2 | |
| α-helix | 108-112 | 5 | |
| α-helix | 139-156 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Von Hippel-Lindau disease tumor suppressor | A | protein | 233 | Homo sapiens | P40337 (AlphaFold model) |
| Transcription elongation factor B polypeptide 2 | B | protein | 118 | Homo sapiens | Q15370 (AlphaFold model) |
| Transcription elongation factor B polypeptide 1 | C | protein | 96 | Homo sapiens | Q15369 (AlphaFold model) |
| Cullin-2 | D | protein | 186 | Homo sapiens | Q13617 (AlphaFold model) |
>4WQO_1 Von Hippel-Lindau disease tumor suppressor (chains A) MGSSHHHHHHSSGLVPRGSHMPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGP EESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPT LPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKE RCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD
>4WQO_2 Transcription elongation factor B polypeptide 2 (chains B) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ
>4WQO_3 Transcription elongation factor B polypeptide 1 (chains C) MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
>4WQO_4 Cullin-2 (chains D) MGSSHHHHHHSQDPTTVKLQAGFMSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWND RFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKG ADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQA ILIRML
Insights into Cullin-RING E3 Ubiquitin Ligase Recruitment: Structure of the VHL-EloBC-Cul2 Complex. Nguyen, H.C., Yang, H., Fribourgh, J.L. et al. Structure (2015) 23:441-449. DOI 10.1016/j.str.2014.12.014 · PubMed
Other PDB entries of the same protein (UniProt P40337 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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