› 2nne

X-ray diffraction
1.6Å resolution

The Structural Identification of the Interaction Site and Functional State of RBP for its Membrane Receptor

Released:
DOI: 10.2210/pdb2nne/pdb
PDB entry 2nne coloured by chain, front view.
PDB entry 2nne coloured by chain, side view.
PDB entry 2nne coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Identification of the retinol-binding protein (RBP) interaction site and functional state of RBPs for the membrane receptor.
Redondo C, Vouropoulou M, Evans J, Findlay JB
FASEB J 22 1043-54 (2008)
PMID: 17991731

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136161 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major urinary protein 6 Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.64 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P02762 (Residues: 19-75, 82-180; Coverage: 96%)
Gene name: Mup6
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

2 bound ligands:
Ligand CD 4 x CD
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P43212
Unit cell:
a: 53.777Å b: 53.777Å c: 137.596Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.24
Expression system: Escherichia coli

Quick links

Citations

7 review citations

New insights and changing paradigms in the regulation of vitamin A metabolism in development.
Shannon et al. (2017)
6 more