› 2fs6

X-ray diffraction
1.35Å resolution

Crystal Structure of Apo-Cellular Retinoic Acid Binding Protein Type II At 1.35 Angstroms Resolution

Released:
DOI: 10.2210/pdb2fs6/pdb
PDB entry 2fs6 coloured by chain, front view.
PDB entry 2fs6 coloured by chain, side view.
PDB entry 2fs6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of Apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation.
Vaezeslami S, Mathes E, Vasileiou C, Borhan B, Geiger JH
J Mol Biol 363 687-701 (2006)
PMID: 16979656

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular retinoic acid-binding protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 137 amino acids
Theoretical weight: 15.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29373 (Residues: 2-138; Coverage: 99%)
Gene name: CRABP2
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

3 bound ligands:
Ligand ACT 7 x ACT
Ligand NA 1 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P1
Unit cell:
a: 34.449Å b: 37.056Å c: 56.527Å
α: 72.68° β: 76.37° γ: 87.28°
R-values:
R R work R free
0.154 0.148 0.204
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Arylfluorosulfate-Based Electrophiles for Covalent Protein Labeling: A New Addition to the Arsenal.
Martín-Gago et al. (2019)
1 more

2 mentions without citation

Arylfluorosulfates Inactivate Intracellular Lipid Binding Protein(s) through Chemoselective SuFEx Reaction with a Binding Site Tyr Residue.
Chen et al. (2016)
1 more