› 2lwp

Solution NMR

The NMR solution structure of the the ubiquitin homology domain of mouse BAG-1

Released:
DOI: 10.2210/pdb2lwp/pdb
PDB entry 2lwp coloured by chain, ensemble of 18 models, front view.
PDB entry 2lwp coloured by chain, ensemble of 18 models, side view.
PDB entry 2lwp coloured by chain, ensemble of 18 models, top view.
Source organism: Mus musculus
Primary publication:
The NMR solution structure of the ubiquitin homology domain of Bcl-2-associated athanogene 1 (BAG-1-UBH) from Mus musculus.
Huang HW, Yu C
Biochem Biophys Res Commun 431 86-91 (2013)
PMID: 23277101

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-178810 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BAG family molecular chaperone regulator 1 Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.8 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q60739 (Residues: 137-233; Coverage: 27%)
Gene name: Bag1
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 88%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Structure and function of a fungal adhesin that binds heparin and mimics thrombospondin-1 by blocking T cell activation and effector function.
Brandhorst et al. (2013)