› 3agx

X-ray diffraction
1.85Å resolution

Crystal structure of human Hsp40 Hdj1 peptide-binding domain

Released:
DOI: 10.2210/pdb3agx/pdb
PDB entry 3agx coloured by chain, front view.
PDB entry 3agx coloured by chain, side view.
PDB entry 3agx 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

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150553 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21
Unit cell:
a: 103.252Å b: 40.921Å c: 62.65Å
α: 90° β: 96.62° γ: 90°
R-values:
R R work R free
0.229 0.228 0.247
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

6 mentions without citation

DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios.
Månsson et al. (2014)
5 more