6EFK: Human CHIP TPR domain

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.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
4
Atoms
2,501
Mol. weight
31.73 kDa
Released
31 Jul 2019

Explore 6EFK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix26-3813
α-helix42-5514
α-helix60-7213
α-helix76-8914
α-helix94-10613
α-helix110-12617
α-helix134-15118
Chain B: 7 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix26-3813
α-helix42-5514
α-helix60-7213
α-helix76-8914
α-helix94-10613
α-helix110-12718
α-helix134-15320

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase CHIPA, Bprotein132Homo sapiensQ9UNE7 (AlphaFold model)
Ace-ile-glu-glu-val-aspC, Dprotein6Homo sapiens
Sequence of entity 1 (A, B), FASTA
>6EFK_1 E3 ubiquitin-protein ligase CHIP (chains A, B)
SPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALAD
CRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIA
KKKRWNSIEERR
Sequence of entity 2 (C, D), FASTA
>6EFK_2 ACE-ILE-GLU-GLU-VAL-ASP (chains C, D)
XIEEVD

Primary citation

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:

Browse structure collections

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