› 5xi9

Solution NMR

Solution structure for human HSP70 substrate binding domain

Released:
DOI: 10.2210/pdb5xi9/pdb
PDB entry 5xi9 coloured by chain, ensemble of 10 models, front view.
PDB entry 5xi9 coloured by chain, ensemble of 10 models, side view.
PDB entry 5xi9 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication.
Umehara K, Hoshikawa M, Tochio N, Tate SI
Molecules 23 (2018)
PMID: 29495458

Function and Biology Details

Biochemical function:
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: 185 amino acids
Theoretical weight: 20.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 381-564; Coverage: 29%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 86%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling.
Genest et al. (2019)
2 more

1 mention without citation

Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication.
Umehara et al. (2018)