› 2qld

X-ray diffraction
2.7Å resolution

human Hsp40 Hdj1

Released:
DOI: 10.2210/pdb2qld/pdb
PDB entry 2qld coloured by chain, front view.
PDB entry 2qld coloured by chain, side view.
PDB entry 2qld coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1.
Hu J, Wu Y, Li J, Qian X, Fu Z, Sha B
BMC Struct Biol 8 3 (2008)
PMID: 18211704

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 Chain: A
Molecule details ›
Chain: A
Length: 183 amino acids
Theoretical weight: 20.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P25685 (Residues: 158-340; Coverage: 54%)
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: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 97.01Å b: 191.13Å c: 40.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.283 0.283 0.336
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Heat shock protein 40: structural studies and their functional implications.
Li et al. (2009)
5 more

9 mentions without citation

The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones.
Velasco et al. (2019)
8 more