› 1p8u

X-ray diffraction
1.62Å resolution

BACTERIORHODOPSIN N' INTERMEDIATE AT 1.62 A RESOLUTION

Released:
DOI: 10.2210/pdb1p8u/pdb
PDB entry 1p8u coloured by chain, ensemble of 2 models, front view.
PDB entry 1p8u coloured by chain, ensemble of 2 models, side view.
PDB entry 1p8u coloured by chain, ensemble of 2 models, top view.
Source organism: Halobacterium salinarum
Primary publication:
Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base.
Schobert B, Brown LS, Lanyi JK
J Mol Biol 330 553-70 (2003)
PMID: 12842471

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacteriorhodopsin Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 26.9 KDa
Source organism: Halobacterium salinarum
Expression system: Halobacterium salinarum
UniProt:
  • Canonical: P02945 (Residues: 14-262; Coverage: 95%)
Gene names: VNG_1467G, bop
Sequence domains: Bacteriorhodopsin-like protein
Structure domains: Rhodopsin 7-helix transmembrane proteins

Ligands and Environments

3 bound ligands:
Ligand RET 1 x RET
Ligand LI1 13 x LI1
Ligand SQU 1 x SQU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P63
Unit cell:
a: 60.981Å b: 60.981Å c: 108.312Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 not available 0.206
Expression system: Halobacterium salinarum

Quick links

Citations

17 review citations

Water in nonpolar confinement: from nanotubes to proteins and beyond.
Rasaiah et al. (2008)
16 more

12 mentions without citation

A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes.
Caffrey M. (2015)
11 more