› 1bct

Solution NMR

THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA IN SOLUTION

Released:
DOI: 10.2210/pdb1bct/pdb
PDB entry 1bct coloured by chain, ensemble of 14 models, front view.
PDB entry 1bct coloured by chain, ensemble of 14 models, side view.
PDB entry 1bct coloured by chain, ensemble of 14 models, top view.
Source organism: Halobacterium salinarum
Primary publication:
Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution.
Barsukov IL, Nolde DE, Lomize AL, Arseniev AS
Eur J Biochem 206 665-72 (1992)
PMID: 1606953

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacteriorhodopsin Chain: A
Molecule details ›
Chain: A
Length: 69 amino acids
Theoretical weight: 7.54 KDa
Source organism: Halobacterium salinarum
Expression system: Not provided
UniProt:
  • Canonical: P02945 (Residues: 176-244; Coverage: 26%)
Gene names: VNG_1467G, bop
Sequence domains: Bacteriorhodopsin-like protein
Structure domains: Bacteriorhodopsin Fragment

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

7 review citations

Solution NMR of membrane proteins: practice and challenges.
Sanders et al. (2006)
6 more

1 mention without citation

The topomer-sampling model of protein folding.
Debe et al. (1999)