› 2d9d

Solution NMR

Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5

Released:
DOI: 10.2210/pdb2d9d/pdb
PDB entry 2d9d coloured by chain, ensemble of 20 models, front view.
PDB entry 2d9d coloured by chain, ensemble of 20 models, side view.
PDB entry 2d9d coloured by chain, ensemble of 20 models, 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193900 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BAG family molecular chaperone regulator 5 Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 9.84 KDa
Source organism: Homo sapiens
Expression system: cell free protein synthesis
UniProt:
  • Canonical: Q9UL15 (Residues: 275-350; Coverage: 17%)
Gene names: BAG5, KIAA0873
Sequence domains: BAG domain
Structure domains: BAG domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: cell free protein synthesis

Quick links

Citations

14 review citations

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

1 mention without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)