8GCK: Human CHIP-TPR domain

Crystal structure of the human CHIP-TPR domain in complex with a 6mer acetylated tau peptide. Determined by X-ray diffraction at 1.37 Å resolution. Released 6 Mar 2024.

Method
X-ray diffraction
Resolution
1.37 Å
Organism
Homo sapiens
Chains
4
Atoms
2,394
Mol. weight
30.74 kDa
Released
6 Mar 2024

Explore 8GCK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8GCK contains 14 α-helices and 2 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-helix27-3913
α-helix43-5614
α-helix61-7313
α-helix77-9014
α-helix95-10713
α-helix111-12717
α-helix135-14915
Chain B: 7 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix27-3913
α-helix43-5614
α-helix61-7313
α-helix77-9014
α-helix95-10713
α-helix111-12717
β-strand13211
β-strand13411
α-helix135-14915

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase CHIPA, Bprotein128Homo sapiensQ9UNE7 (AlphaFold model)
Ace-ser-ile-asp-met-val-aspC, Eprotein7Homo sapiensP10636 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>8GCK_1 E3 ubiquitin-protein ligase CHIP (chains A, B)
KSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALA
DCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRI
AKKKRWNS
Sequence of entity 2 (C, E), FASTA
>8GCK_2 ACE-SER-ILE-ASP-MET-VAL-ASP (chains C, E)
XSIDMVD

Primary citation

Intersecting PTMS regulate clearance of pathogenic tau by the CHIP ubiquitin ligase. Nadel, C.M., Gestwicki, J.E. Alzheimer's Dement (2022) 18. DOI 10.1002/alz.062036

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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