› 2hzr

X-ray diffraction
1.8Å resolution

Crystal structure of human apolipoprotein D (ApoD)

Released:
DOI: 10.2210/pdb2hzr/pdb
PDB entry 2hzr coloured by chain, front view.
PDB entry 2hzr coloured by chain, side view.
PDB entry 2hzr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D.
Eichinger A, Nasreen A, Kim HJ, Skerra A
J Biol Chem 282 31068-75 (2007)
PMID: 17699160

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-138418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein D Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 19.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05090 (Residues: 23-189; Coverage: 99%)
Gene name: APOD
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 49.247Å b: 49.247Å c: 143.486Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.202 0.25
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Alternative binding proteins: anticalins - harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities.
Skerra A. (2008)
9 more

7 mentions without citation

Amphipathic α-helices in apolipoproteins are crucial to the formation of infectious hepatitis C virus particles.
Fukuhara et al. (2014)
6 more