› 1pxr

X-ray diffraction
1.7Å resolution

Structure of Pro50Ala mutant of Bacteriorhodopsin

Released:
DOI: 10.2210/pdb1pxr/pdb
PDB entry 1pxr coloured by chain, front view.
PDB entry 1pxr coloured by chain, side view.
PDB entry 1pxr coloured by chain, top view.
Source organism: Halobacterium salinarum
Primary publication:
Side-chain contributions to membrane protein structure and stability.
Faham S, Yang D, Bare E, Yohannan S, Whitelegge JP, Bowie JU
J Mol Biol 335 297-305 (2004)
PMID: 14659758

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 Chains: A, B
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand RET 2 x RET
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 44.967Å b: 108.839Å c: 55.981Å
α: 90° β: 113.6° γ: 90°
R-values:
R R work R free
0.209 0.207 0.246
Expression system: Halobacterium salinarum

Quick links

Citations

30 review citations

Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs.
Senes et al. (2004)
29 more

4 mentions without citation

Quantification of helix-helix binding affinities in micelles and lipid bilayers.
Lomize et al. (2004)
3 more