› 3a8y

X-ray diffraction
2.3Å resolution

Crystal structure of the complex between the BAG5 BD5 and Hsp70 NBD

Released:
DOI: 10.2210/pdb3a8y/pdb
PDB entry 3a8y coloured by chain, front view.
PDB entry 3a8y coloured by chain, side view.
PDB entry 3a8y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.
Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S
Structure 18 309-19 (2010)
PMID: 20223214

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143652 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Heat shock 70 kDa protein 1A Chains: A, B
Molecule details ›
Chains: A, B
Length: 392 amino acids
Theoretical weight: 43.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 1-388; Coverage: 61%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein
Structure domains:
BAG family molecular chaperone regulator 5 Chains: C, D
Molecule details ›
Chains: C, D
Length: 142 amino acids
Theoretical weight: 16.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UL15 (Residues: 341-447; Coverage: 24%)
Gene names: BAG5, KIAA0873
Sequence domains: BAG domain
Structure domains: BAG domain

Ligands and Environments

1 bound ligand:
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 64.108Å b: 84.266Å c: 96.632Å
α: 90° β: 100.73° γ: 90°
R-values:
R R work R free
0.218 0.218 0.281
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
13 more

4 mentions without citation

Unraveling the essential role of CysK in CDI toxin activation.
Johnson et al. (2016)
3 more