› 5hzq

X-ray diffraction
1.75Å resolution

Crystal structure of cellular retinoic acid binding protein 2 (CRABP2)-aryl fluorosulfate covalent conjugate

Released:
DOI: 10.2210/pdb5hzq/pdb
PDB entry 5hzq coloured by chain, front view.
PDB entry 5hzq coloured by chain, side view.
PDB entry 5hzq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Arylfluorosulfates Inactivate Intracellular Lipid Binding Protein(s) through Chemoselective SuFEx Reaction with a Binding Site Tyr Residue.
Chen W, Dong J, Plate L, Mortenson DE, Brighty GJ, Li S, Liu Y, Galmozzi A, Lee PS, Hulce JJ, Cravatt BF, Saez E, Powers ET, Wilson IA, Sharpless KB, Kelly JW
J Am Chem Soc 138 7353-64 (2016)
PMID: 27191344

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-151430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cellular retinoic acid-binding protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 140 amino acids
Theoretical weight: 15.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29373 (Residues: 1-138; Coverage: 100%)
Gene name: CRABP2
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

2 bound ligands:
Ligand YWZ 2 x YWZ
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P212121
Unit cell:
a: 37.029Å b: 89.732Å c: 92.463Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.228
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Click Chemistry in Proteomic Investigations.
Parker et al. (2020)
23 more

2 mentions without citation

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