› 1cbi

X-ray diffraction
2.7Å resolution

APO-CELLULAR RETINOIC ACID BINDING PROTEIN I

Released:
DOI: 10.2210/pdb1cbi/pdb
PDB entry 1cbi coloured by chain, front view.
PDB entry 1cbi coloured by chain, side view.
PDB entry 1cbi coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet.
Thompson JR, Bratt JM, Banaszak LJ
J Mol Biol 252 433-46 (1995)
PMID: 7563063

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158819 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular retinoic acid-binding protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 136 amino acids
Theoretical weight: 15.48 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P62965 (Residues: 2-137; Coverage: 99%)
Gene name: Crabp1
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 127.45Å b: 127.45Å c: 53.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.233
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Retinoid-binding proteins: mediators of retinoid action.
Noy N. (2000)
3 more

22 mentions without citation

Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm.
McGuffee et al. (2010)
21 more