› 4qyn

X-ray diffraction
1.19Å resolution

The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinol

Released:
DOI: 10.2210/pdb4qyn/pdb
PDB entry 4qyn coloured by chain, front view.
PDB entry 4qyn coloured by chain, side view.
PDB entry 4qyn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of holo wild-type human cellular retinol-binding protein II (hCRBPII) bound to retinol and retinal.
Nossoni Z, Assar Z, Yapici I, Nosrati M, Wang W, Berbasova T, Vasileiou C, Borhan B, Geiger J
Acta Crystallogr D Biol Crystallogr 70 3226-32 (2014)
PMID: 25478840

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Retinol-binding protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 133 amino acids
Theoretical weight: 15.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50120 (Residues: 2-134; Coverage: 99%)
Gene names: CRBP2, RBP2
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

2 bound ligands:
Ligand RTL 2 x RTL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 34.65Å b: 75.147Å c: 54.65Å
α: 90° β: 100.79° γ: 90°
R-values:
R R work R free
0.189 0.187 0.216
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Retinol-binding protein 2 (RBP2): biology and pathobiology.
Blaner et al. (2020)
2 more

2 mentions without citation

Functional characterisation of substrate-binding proteins to address nutrient uptake in marine picocyanobacteria.
Ford et al. (2021)
1 more