RNF38-UbcH5B-UB complex. Determined by X-ray diffraction at 2.04 Å resolution. Released 8 Apr 2015.
Explore 4V3K in 3D Show helices and sheets RCSB PDB PDBe
4V3K contains 29 α-helices and 48 β-strands across 6 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 | 3-15 | 13 | |
| α-helix | 17-18 | 2 | |
| β-strand | 21-24 | 4 | 1 |
| β-strand | 32-38 | 7 | 1 |
| α-helix | 39-40 | 2 | |
| β-strand | 49-55 | 7 | 1 |
| α-helix | 64-65 | 2 | |
| β-strand | 66-69 | 4 | 1 |
| β-strand | 75 | 1 | 2 |
| β-strand | 78 | 1 | 2 |
| β-strand | 83 | 1 | 1 |
| β-strand | 84 | 1 | 2 |
| β-strand | 86 | 1 | 3 |
| α-helix | 87-89 | 3 | |
| α-helix | 99-111 | 13 | |
| α-helix | 121-129 | 9 | |
| α-helix | 131-145 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 4 |
| β-strand | 12-17 | 6 | 4 |
| β-strand | 22 | 1 | 5 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 4 |
| β-strand | 48-49 | 2 | 4 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 5 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-71 | 6 | 4 |
| β-strand | 75 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 391-395 | 5 | |
| β-strand | 398-400 | 3 | 6 |
| β-strand | 412-413 | 2 | 7 |
| β-strand | 418-419 | 2 | 7 |
| α-helix | 424 | 1 | |
| β-strand | 425-428 | 4 | 6 |
| β-strand | 434-436 | 3 | 6 |
| α-helix | 437-446 | 10 | |
| β-strand | 449 | 1 | 8 |
| β-strand | 456 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| β-strand | 21-25 | 5 | 9 |
| β-strand | 32-38 | 7 | 9 |
| α-helix | 39-40 | 2 | |
| β-strand | 49-55 | 7 | 9 |
| α-helix | 64-65 | 2 | |
| β-strand | 66-69 | 4 | 9 |
| β-strand | 75 | 1 | 10 |
| β-strand | 78 | 1 | 10 |
| β-strand | 83 | 1 | 9 |
| β-strand | 84 | 1 | 10 |
| β-strand | 86 | 1 | 11 |
| α-helix | 87-89 | 3 | |
| α-helix | 99-110 | 12 | |
| α-helix | 121-129 | 9 | |
| α-helix | 131-145 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 D2 | A, D | protein | 146 | HOMO SAPIENS | P62837 (AlphaFold model) |
| Polyubiquitin-C | B, E | protein | 81 | HOMO SAPIENS | P0CG48 (AlphaFold model) |
| E3 ubiquitin-protein ligase RNF38 | C, F | protein | 79 | HOMO SAPIENS | Q9H0F5 (AlphaFold model) |
>4V3K_1 UBIQUITIN-CONJUGATING ENZYME E2 D2 (chains A, D) ALKRIHKELNDLARDPPAQCRAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYP FKPPKVAFTTRIYHPNINSNGSIKLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVP EIARIYKTDREKYNRIAREWTQKYAM
>4V3K_2 POLYUBIQUITIN-C (chains B, E) GSGGSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRT LSDYNIQKESTLHLVLRLRGG
>4V3K_3 E3 UBIQUITIN-PROTEIN LIGASE RNF38 (chains C, F) GSTKADIEQLPSYRFNPNNHQSEQTLCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKA NRTCPICRADASEVHRDSE
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Water and common crystallization additives (EDO, CL) are not listed.
Activation of a Primed Ring E3-E2-Ubiquitin Complex by Non-Covalent Ubiquitin. Buetow, L., Gabrielsen, M., Anthony, N.G. et al. Mol Cell (2015) 58:297. DOI 10.1016/J.MOLCEL.2015.02.017 · PubMed
Other PDB entries of the same protein (UniProt P62837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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