Crystal structure of SOCS2:Elongin C:Elongin B in complex with erythropoietin receptor peptide. Determined by X-ray diffraction at 2.69 Å resolution. Released 29 May 2019.
Explore 6I4X in 3D Show helices and sheets RCSB PDB PDBe
6I4X contains 18 α-helices and 26 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 | 32-46 | 15 | |
| β-strand | 49 | 1 | 6 |
| α-helix | 55-61 | 7 | |
| α-helix | 66 | 1 | |
| β-strand | 70-74 | 5 | 6 |
| β-strand | 82-88 | 7 | 6 |
| β-strand | 91-100 | 10 | 6 |
| β-strand | 103-106 | 4 | 6 |
| β-strand | 108 | 1 | 7 |
| β-strand | 119 | 1 | 6 |
| α-helix | 122-132 | 11 | |
| β-strand | 155 | 1 | 6 |
| α-helix | 160-162 | 3 | |
| α-helix | 163-172 | 10 | |
| α-helix | 185-192 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 12-19 | 8 | 1 |
| β-strand | 23 | 1 | 3 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 49-50 | 2 | 1 |
| β-strand | 56 | 1 | 3 |
| β-strand | 68 | 1 | 4 |
| β-strand | 71 | 1 | 4 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 1 |
| β-strand | 80-81 | 2 | 5 |
| β-strand | 84-85 | 2 | 5 |
| α-helix | 86-87 | 2 | |
| β-strand | 90 | 1 | 2 |
| α-helix | 91-94 | 4 | |
| α-helix | 98-100 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-44 | 5 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 67-82 | 16 | |
| α-helix | 89-92 | 4 | |
| α-helix | 97-110 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 0 | 1 | 6 |
| β-strand | 3 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Elongin-B | B | protein | 104 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin-C | C | protein | 97 | Homo sapiens | Q15369 (AlphaFold model) |
| Suppressor of cytokine signaling 2 | A | protein | 169 | Homo sapiens | O14508 (AlphaFold model) |
| Erythropoietin receptor | D | protein | 11 | Homo sapiens |
>6I4X_1 Elongin-B (chains B) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
>6I4X_2 Elongin-C (chains C) MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
>6I4X_3 Suppressor of cytokine signaling 2 (chains A) SMQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTS AGPTNLRIEYQDGKFRLDSIICVKSALAAFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVH LYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV
>6I4X_4 Erythropoietin receptor (chains D) ASFEYTILDPS
Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase. Kung, W.W., Ramachandran, S., Makukhin, N. et al. Nat Commun (2019) 10:2534-2534. DOI 10.1038/s41467-019-10190-4 · PubMed
Other PDB entries of the same protein (UniProt Q15370 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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