› 4psq

X-ray diffraction
2.4Å resolution

Crystal Structure of Retinol-Binding Protein 4 (RBP4) in complex with a non-retinoid ligand

Released:
DOI: 10.2210/pdb4psq/pdb
PDB entry 4psq coloured by chain, front view.
PDB entry 4psq coloured by chain, side view.
PDB entry 4psq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-assisted discovery of the first non-retinoid ligands for Retinol-Binding Protein 4.
Wang Y, Connors R, Fan P, Wang X, Wang Z, Liu J, Kayser F, Medina JC, Johnstone S, Xu H, Thibault S, Walker N, Conn M, Zhang Y, Liu Q, Grillo MP, Motani A, Coward P, Wang Z
Bioorg Med Chem Lett 24 2885-91 (2014)
PMID: 24835984

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-136146 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Retinol-binding protein 4 Chains: A, B
Molecule details ›
Chains: A, B
Length: 212 amino acids
Theoretical weight: 24.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02753 (Residues: 19-201; Coverage: 100%)
Gene names: PRO2222, RBP4
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

3 bound ligands:
Ligand 2WL 2 x 2WL
Ligand PO4 2 x PO4
Ligand EDO 20 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P65
Unit cell:
a: 96.531Å b: 96.531Å c: 118.072Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.242 0.287
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Retinol-binding protein-4 and hs-CRP levels in patients with migraine.
Tanik et al. (2015)
5 more

1 mention without citation

Design, Synthesis, and Preclinical Efficacy of Novel Nonretinoid Antagonists of Retinol-Binding Protein 4 in the Mouse Model of Hepatic Steatosis.
Cioffi et al. (2019)