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Crystal structure of human Hsp40 Hdj1 peptide-binding domain complexed with a C-terminal peptide of Hsp70

Source organism: Homo sapiens
Biochemical function: unfolded protein binding
Biological process: protein folding
Cellular component: not assigned

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EC 3.6.4.10: Non-chaperonin molecular chaperone ATPase

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Systematic name:
ATP phosphohydrolase (polypeptide-polymerizing)
Alternative Name(s):
  • Molecular chaperone Hsc70 ATPase

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF01556
Domain description: DnaJ C terminal domain
Occurring in:
  1. DnaJ homolog subfamily B member 1
The deposited structure of PDB entry 3agy contains 2 copies of Pfam domain PF01556 (DnaJ C terminal domain) in DnaJ homolog subfamily B member 1. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR008971
Domain description: HSP40/DnaJ peptide-binding
Occurring in:
  1. DnaJ homolog subfamily B member 1
IPR002939
Domain description: Chaperone DnaJ, C-terminal
Occurring in:
  1. DnaJ homolog subfamily B member 1

Structure domain

CATH CATH domain
2.60.260.20
Class: Mainly Beta
Architecture: Sandwich
Topology: HSP40/DNAj peptide-binding domain
Homology: Urease metallochaperone UreE, N-terminal domain
Occurring in:
  1. DnaJ homolog subfamily B member 1
The deposited structure of PDB entry 3agy contains 4 copies of CATH domain 2.60.260.20 (HSP40/DNAj peptide-binding domain) in DnaJ homolog subfamily B member 1. Showing 2 copies in chain A.

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