CHIP-TPR in complex with the C-terminus of CHIC2. Determined by X-ray diffraction at 1.63 Å resolution. Released 20 Mar 2024.
Explore 8SUV in 3D Show helices and sheets RCSB PDB PDBe
8SUV contains 28 α-helices and 0 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 | 26-38 | 13 | |
| α-helix | 42-55 | 14 | |
| α-helix | 60-72 | 13 | |
| α-helix | 76-89 | 14 | |
| α-helix | 94-106 | 13 | |
| α-helix | 110-126 | 17 | |
| α-helix | 134-148 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-38 | 13 | |
| α-helix | 42-55 | 14 | |
| α-helix | 60-72 | 13 | |
| α-helix | 76-89 | 14 | |
| α-helix | 94-106 | 13 | |
| α-helix | 110-126 | 17 | |
| α-helix | 134-149 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-38 | 13 | |
| α-helix | 42-55 | 14 | |
| α-helix | 60-72 | 13 | |
| α-helix | 76-89 | 14 | |
| α-helix | 94-106 | 13 | |
| α-helix | 110-127 | 18 | |
| α-helix | 134-149 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase CHIP | A, B, C, D | protein | 139 | Homo sapiens | Q9UNE7 (AlphaFold model) |
| Cysteine-rich hydrophobic domain-containing protein 2 | F, G, H, I | protein | 12 | Homo sapiens | Q9UKJ5 (AlphaFold model) |
>8SUV_1 E3 ubiquitin-protein ligase CHIP (chains A, B, C, D) GAMGSEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQ HEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDI PSALRIAKKKRWNSIEERR
>8SUV_2 Cysteine-rich hydrophobic domain-containing protein 2 (chains F, G, H, I) EFLPKTPIFRPD
Interaction with the membrane-anchored protein CHIC2 constrains the ubiquitin ligase activity of CHIP. Callahan, M., Hodul, M., Carroll, E. et al. bioRxiv (2023). DOI 10.1101/2023.07.17.549407
Other PDB entries of the same protein (UniProt Q9UNE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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