› 5nty

X-ray diffraction
2Å resolution

Structure of non-fluorescent human plasma RBP4

Released:
DOI: 10.2210/pdb5nty/pdb
PDB entry 5nty coloured by chain, front view.
PDB entry 5nty coloured by chain, side view.
PDB entry 5nty coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human plasma retinol-binding protein (RBP4) is also a fatty acid-binding protein.
Perduca M, Nicolis S, Mannucci B, Galliano M, Monaco HL
Biochim Biophys Acta Mol Cell Biol Lipids 1863 458-466 (2018)
PMID: 29414511

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 Chain: A
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 20.98 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02753 (Residues: 19-200; Coverage: 100%)
Gene names: PRO2222, RBP4
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

2 bound ligands:
Ligand PLM 1 x PLM
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: R3
Unit cell:
a: 103.77Å b: 103.77Å c: 73.94Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.172 0.23

Quick links

Citations

8 review citations

Biological Functions of RBP4 and Its Relevance for Human Diseases.
Steinhoff et al. (2021)
7 more

1 mention without citation

High resolution crystal structure data of human plasma retinol-binding protein (RBP4) bound to retinol and fatty acids.
Perduca et al. (2018)