Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated HSP70 peptide. Determined by X-ray diffraction at 1.5 Å resolution. Released 31 Jul 2019.
Explore 6EFK in 3D Show helices and sheets RCSB PDB PDBe
6EFK contains 14 α-helices and 0 β-strands across 2 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 | 134-151 | 18 |
| 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 | 134-153 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase CHIP | A, B | protein | 132 | Homo sapiens | Q9UNE7 (AlphaFold model) |
| Ace-ile-glu-glu-val-asp | C, D | protein | 6 | Homo sapiens |
>6EFK_1 E3 ubiquitin-protein ligase CHIP (chains A, B) SPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALAD CRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIA KKKRWNSIEERR
>6EFK_2 ACE-ILE-GLU-GLU-VAL-ASP (chains C, D) XIEEVD
Specificity for latent C termini links the E3 ubiquitin ligase CHIP to caspases. Ravalin, M., Theofilas, P., Basu, K. et al. Nat Chem Biol (2019) 15:786-794. DOI 10.1038/s41589-019-0322-6 · PubMed
Other PDB entries of the same protein (UniProt Q9UNE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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