› 3agy

X-ray diffraction
1.85Å resolution

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

Released:
DOI: 10.2210/pdb3agy/pdb
PDB entry 3agy coloured by chain, front view.
PDB entry 3agy coloured by chain, side view.
PDB entry 3agy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Peptide-binding sites as revealed by the crystal structures of the human Hsp40 Hdj1 C-terminal domain in complex with the octapeptide from human Hsp70.
Suzuki H, Noguchi S, Arakawa H, Tokida T, Hashimoto M, Satow Y
Biochemistry 49 8577-84 (2010)
PMID: 20809635

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145681 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DnaJ homolog subfamily B member 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 20.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P25685 (Residues: 161-340; Coverage: 53%)
Gene names: DNAJ1, DNAJB1, HDJ1, HSPF1
Sequence domains: DnaJ C terminal domain
Structure domains: Urease metallochaperone UreE, N-terminal domain
Heat shock cognate 71 kDa protein Chains: C, D, F
Molecule details ›
Chains: C, D, F
Length: 8 amino acids
Theoretical weight: 859 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P11142 (Residues: 639-646; Coverage: 1%)
Gene names: HSC70, HSP73, HSPA10, HSPA8

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 104.746Å b: 41.132Å c: 62.865Å
α: 90° β: 97.42° γ: 90°
R-values:
R R work R free
0.226 0.225 0.247
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

The human HSP70 family of chaperones: where do we stand?
Radons J. (2016)
5 more

7 mentions without citation

ATP-driven molecular chaperone machines.
Clare et al. (2013)
6 more