2QLD

human Hsp40 Hdj1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.336 
  • R-Value Work: 0.283 
  • R-Value Observed: 0.283 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

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.

(2008) BMC Struct Biol 8: 3-3

  • DOI: https://doi.org/10.1186/1472-6807-8-3
  • Primary Citation of Related Structures:  
    2QLD

  • PubMed Abstract: 

    The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question. How Hsp40 co-operates with Hsp70 to facilitate protein folding is not well understood. To investigate the mechanisms, we determined the crystal structure of the putative peptide-binding fragment of Hdj1, a human member of the type II Hsp40 family.


  • Organizational Affiliation

    Department of Cell Biology, University of Alabama at Birmingham, Birmingham, AL 35294, USA. hujunbin@uab.edu


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DnaJ homolog subfamily B member 1183Homo sapiensMutation(s): 0 
Gene Names: DNAJB1DNAJ1HDJ1HSPF1
UniProt & NIH Common Fund Data Resources
Find proteins for P25685 (Homo sapiens)
Explore P25685 
Go to UniProtKB:  P25685
PHAROS:  P25685
GTEx:  ENSG00000132002 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25685
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.336 
  • R-Value Work: 0.283 
  • R-Value Observed: 0.283 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 97.01α = 90
b = 191.13β = 90
c = 40.96γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
EPMRphasing
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-07-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references