› 2lmg

Solution NMR

Solution Structure of The C-terminal Domain (537-610) of Human Heat Shock Protein 70

Released:
DOI: 10.2210/pdb2lmg/pdb
PDB entry 2lmg coloured by chain, ensemble of 20 models, front view.
PDB entry 2lmg coloured by chain, ensemble of 20 models, side view.
PDB entry 2lmg coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation.
Gao XC, Zhou CJ, Zhou ZR, Wu M, Cao CY, Hu HY
J Biol Chem 287 6044-52 (2012)
PMID: 22219199

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock 70 kDa protein 1A Chain: A
Molecule details ›
Chain: A
Length: 75 amino acids
Theoretical weight: 8.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 537-610; Coverage: 12%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Structure domains: Substrate Binding Domain Of Dnak; Chain:A; Domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

3 review citations

HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
Stricher et al. (2013)
2 more

6 mentions without citation

Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate.
Zhang et al. (2014)
5 more