4KBQ: CHIP-TPR domain

Structure of the CHIP-TPR domain in complex with the Hsc70 Lid-Tail domains. Determined by X-ray diffraction at 2.91 Å resolution. Released 14 Jan 2015.

Method: X-ray diffraction
Resolution: 2.91 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,559
Mol. weight: 54.62 kDa
Released: 14 Jan 2015

Explore 4KBQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4KBQ contains 22 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.

Chain A: 7 helices, 0 β-strands

Element	Residues	Length
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	134-147	14

Chain B: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	26-38	13
α-helix	42-55	14
α-helix	60-72	13
α-helix	76-89	14
α-helix	94-105	12
α-helix	110-127	18
α-helix	134-147	14

Chain C: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	536-553	18
α-helix	556-558	3
α-helix	564-583	20
α-helix	589-611	23

Chain D: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	536-556	21
α-helix	564-582	19
α-helix	594-612	19
α-helix	613-616	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
E3 ubiquitin-protein ligase CHIP	A, B	protein	139	Homo sapiens	Q9UNE7 (AlphaFold model)
Heat shock cognate 71 kDa protein	C, D	protein	101	Homo sapiens	P11142 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4KBQ_1 E3 ubiquitin-protein ligase CHIP (chains A, B)
GAMGSEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQ
HEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDI
PSALRIAKKKRWNSIEERR

Sequence of entity 2 (C, D), FASTA

>4KBQ_2 Heat shock cognate 71 kDa protein (chains C, D)
GIDPFTEFSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEF
EHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFGPTIEEVD

Primary citation

A Bipartite Interaction between Hsp70 and CHIP Regulates Ubiquitination of Chaperoned Client Proteins. Zhang, H., Amick, J., Chakravarti, R. et al. Structure (2015) 23:472-482. DOI 10.1016/j.str.2015.01.003 · PubMed

Other PDB entries of the same protein (UniProt Q9UNE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9QFY 1.06 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 9.
6NSV 1.3 Å, Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated…
9QFS 1.33 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 8.
9QEU 1.35 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 1
8GCK 1.37 Å, Crystal structure of the human CHIP-TPR domain in complex with a 6mer acetylated tau…
8EI0 1.47 Å, Crystal structure of the STUB1 TPR domain in complex with H318, a Helicon Polypeptide
6EFK 1.5 Å, Crystal structure of the human CHIP TPR domain in complex with a 5mer acetylated HSP70…
9QF1 1.51 Å, Structure of CHIP E3 ubiquitin ligase TPR domain in complex with compound 2
8F16 1.56 Å, Structure of the STUB1 TPR domain in complex with H203, an all-D Helicon Polypeptide
9DYB 1.6 Å, CHIP-TPR in complex with the phosphorylated Hsp70 tail
8SUV 1.63 Å, CHIP-TPR in complex with the C-terminus of CHIC2
8F14 1.69 Å, Structure of the STUB1 TPR domain in complex with H201, an all-D Helicon Polypeptide

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