› 2ei4

X-ray diffraction
2.1Å resolution

Trimeric complex of archaerhodopsin-2

Released:
DOI: 10.2210/pdb2ei4/pdb
PDB entry 2ei4 coloured by chain, front view.
PDB entry 2ei4 coloured by chain, side view.
PDB entry 2ei4 coloured by chain, top view.
Source organism: Halobacterium sp. AUS-2
Primary publication:
Structural role of bacterioruberin in the trimeric structure of archaerhodopsin-2.
Yoshimura K, Kouyama T
J Mol Biol 375 1267-81 (2008)
PMID: 18082767

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Archaerhodopsin-2 Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 27.31 KDa
Source organism: Halobacterium sp. AUS-2
UniProt:
  • Canonical: P29563 (Residues: 7-259; Coverage: 98%)
Sequence domains: Bacteriorhodopsin-like protein
Structure domains: Rhodopsin 7-helix transmembrane proteins

Ligands and Environments

4 bound ligands:
Ligand GLC 1 x GLC
Ligand RET 1 x RET
Ligand 22B 1 x 22B
Ligand L2P 1 x L2P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P321
Unit cell:
a: 98.16Å b: 98.16Å c: 56.16Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.197

Quick links

Citations

11 review citations

Carotenoids from Haloarchaea and Their Potential in Biotechnology.
Rodrigo-Baños et al. (2015)
10 more

12 mentions without citation

Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.
Dong et al. (2012)
11 more