6I5J: SOCS2:Elongin C:Elongin B
Crystal structure of SOCS2:Elongin C:Elongin B in complex with growth hormone receptor peptide. Determined by X-ray diffraction at 2.8 Å resolution. Released 29 May 2019.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 6,135
- Mol. weight
- 89.91 kDa
- Ligands
- CO
- Released
- 29 May 2019
Explore 6I5J in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6I5J contains 46 α-helices and 58 β-strands across 10 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.
Chain A: 11 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 32-46 | 15 | |
| β-strand | 49 | 1 | 1 |
| α-helix | 55-61 | 7 | |
| α-helix | 66 | 1 | |
| β-strand | 70-74 | 5 | 1 |
| β-strand | 82-88 | 7 | 1 |
| β-strand | 91-100 | 10 | 1 |
| β-strand | 103-106 | 4 | 1 |
| β-strand | 108 | 1 | 2 |
| α-helix | 113-115 | 3 | |
| β-strand | 119 | 1 | 1 |
| α-helix | 122-132 | 11 | |
| α-helix | 148 | 1 | |
| β-strand | 149 | 1 | 2 |
| α-helix | 150 | 1 | |
| β-strand | 155 | 1 | 1 |
| α-helix | 160-162 | 3 | |
| α-helix | 163-172 | 10 | |
| α-helix | 178-180 | 3 | |
| α-helix | 185-192 | 8 | |
Chain B: 8 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 3 |
| β-strand | 10 | 1 | 4 |
| β-strand | 12-19 | 8 | 3 |
| β-strand | 23 | 1 | 5 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 3 |
| β-strand | 49-50 | 2 | 3 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 5 |
| α-helix | 57-60 | 4 | |
| β-strand | 68 | 1 | 6 |
| β-strand | 71 | 1 | 6 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 3 |
| β-strand | 80-81 | 2 | 7 |
| β-strand | 84-85 | 2 | 7 |
| α-helix | 86-88 | 3 | |
| β-strand | 90 | 1 | 4 |
| α-helix | 91-94 | 4 | |
| α-helix | 96-100 | 5 | |
Chain C: 4 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 3 |
| β-strand | 28-32 | 5 | 3 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-46 | 7 | |
| β-strand | 56-57 | 2 | 8 |
| β-strand | 59-61 | 3 | 3 |
| α-helix | 67-82 | 16 | |
| α-helix | 97-110 | 14 | |
Chain D: 10 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 32-46 | 15 | |
| β-strand | 49 | 1 | 9 |
| α-helix | 55-61 | 7 | |
| α-helix | 66 | 1 | |
| β-strand | 70-74 | 5 | 9 |
| β-strand | 82-88 | 7 | 9 |
| β-strand | 91-100 | 10 | 9 |
| β-strand | 103-106 | 4 | 9 |
| β-strand | 108 | 1 | 10 |
| α-helix | 110-112 | 3 | |
| β-strand | 119 | 1 | 9 |
| α-helix | 122-132 | 11 | |
| α-helix | 133-135 | 3 | |
| β-strand | 148-149 | 2 | 10 |
| α-helix | 150 | 1 | |
| β-strand | 155 | 1 | 9 |
| α-helix | 163-174 | 12 | |
| α-helix | 178-180 | 3 | |
| α-helix | 185-192 | 8 | |
Chain E: 7 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 11 |
| β-strand | 10 | 1 | 12 |
| β-strand | 12-19 | 8 | 11 |
| β-strand | 23 | 1 | 13 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 11 |
| β-strand | 49-50 | 2 | 11 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 13 |
| β-strand | 68 | 1 | 14 |
| β-strand | 71 | 1 | 14 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 11 |
| β-strand | 80 | 1 | 15 |
| β-strand | 85 | 1 | 15 |
| α-helix | 86-88 | 3 | |
| β-strand | 90 | 1 | 12 |
| α-helix | 91-94 | 4 | |
| α-helix | 98-100 | 3 | |
Chain F: 5 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 11 |
| β-strand | 28-32 | 5 | 11 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-46 | 7 | |
| β-strand | 55-56 | 2 | 8 |
| β-strand | 59-61 | 3 | 11 |
| α-helix | 67-82 | 16 | |
| α-helix | 89-90 | 2 | |
| α-helix | 100-110 | 11 | |
Chain I: 0 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 0 | 1 | 1 |
| β-strand | 3-5 | 3 | 2 |
Chain J: 0 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 0 | 1 | 9 |
| β-strand | 3 | 1 | 10 |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Suppressor of cytokine signaling 2 | A | protein | 169 | Homo sapiens | O14508 (AlphaFold model) |
| Elongin-B | B, E | protein | 104 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin-C | C, F | protein | 97 | Homo sapiens | Q15369 (AlphaFold model) |
| Suppressor of cytokine signaling 2 | D | protein | 169 | Homo sapiens | O14508 (AlphaFold model) |
| Growth hormone receptor peptide | I, J, K, L | protein | 11 | Homo sapiens | |
Sequence of entity 1 (A), FASTA
>6I5J_1 Suppressor of cytokine signaling 2 (chains A)
SMQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTS
AGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVH
LYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV
Sequence of entity 2 (B, E), FASTA
>6I5J_2 Elongin-B (chains B, E)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMK
Sequence of entity 3 (C, F), FASTA
>6I5J_3 Elongin-C (chains C, F)
MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM
YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 4 (D), FASTA
>6I5J_4 Suppressor of cytokine signaling 2 (chains D)
SMQAARLAKALRELGQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTS
AGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVH
LYLTKPLYTSAPSLQHLCRLTINKCTGAIWGLPLPTRLKDYLEEYKFQV
Sequence of entity 5 (I, J, K, L), FASTA
>6I5J_5 Growth hormone receptor peptide (chains I, J, K, L)
PVPDYTSIHIX
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CO | Cobalt (II) ion | Co | 2 |
Primary citation
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 O14508 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7ZLM 1.79 Å, Crystal structure of SOCS2:ElonginB:ElonginC in complex with compound MN551
- 2C9W 1.9 Å, Crystal structure of socs-2 in complex with elongin-B and elongin-C at 1.9A resolution
- 7ZLS 1.92 Å, co-crystal structure of SOCS2:ElonginB:ElonginC in complex with compound 13
- 7ZLP 1.94 Å, Crystal structure of SOCS2:ElonginB:ElonginC in complex with compound 9
- 6I5N 1.98 Å, Crystal structure of SOCS2:Elongin C:Elongin B in complex with growth hormone receptor…
- 7ZLR 2.01 Å, Crystal structure of SOCS2:ElonginB:ElonginC in complex with compound 13
- 7ZLO 2.22 Å, Crystal structure of SOCS2:ElonginB:ElonginC in complex with compound 12
- 7ZLN 2.6 Å, Crystal structure of SOCS2:ElonginB:ElonginC in complex with compound 11
- 6I4X 2.69 Å, Crystal structure of SOCS2:Elongin C:Elongin B in complex with erythropoietin receptor…
- 5BO4 2.9 Å, Structure of SOCS2:Elongin C:Elongin B from DMSO-treated crystals
- 4JGH 3.0 Å, Structure of the SOCS2-Elongin BC complex bound to an N-terminal fragment of Cullin5
- 7M6T 3.19 Å, Crystal structure of SOCS2/ElonginB/ElonginC bound to a non-canonical peptide that…
Browse structure collections
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