PDBe 2ka2

Solution NMR

Solution NMR structure of BNIP3 transmembrane peptide dimer in detergent micelles with His173-Ser172 intermonomer hydrogen bond restraints

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for dimerization of the BNIP3 transmembrane domain.
Biochemistry 48 5106-20 (2009)
PMID: 19415897

Function and Biology Details

Biochemical function:
  • not assigned
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 35 amino acids
Theoretical weight: 3.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12983 (Residues: 219-253; Coverage: 14%)
Gene names: BNIP3, NIP3

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli