3fsn

X-ray diffraction
2.14Å resolution

Crystal structure of RPE65 at 2.14 angstrom resolution

Released:
Source organism: Bos taurus
Primary publication:
Crystal structure of native RPE65, the retinoid isomerase of the visual cycle.
Proc Natl Acad Sci U S A 106 17325-30 (2009)
PMID: 19805034

Function and Biology Details

Reactions catalysed:
An all-trans-retinyl ester + H(2)O = 11-cis-retinol + a fatty acid
Lutein = meso-zeaxanthin
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-173309 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Retinoid isomerohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 533 amino acids
Theoretical weight: 61.04 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q28175 (Residues: 1-533; Coverage: 100%)
Gene name: RPE65
Sequence domains: Retinal pigment epithelial membrane protein

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P65
Unit cell:
a: 176.516Å b: 176.516Å c: 86.862Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.182 0.18 0.216