› 2xkl

X-ray diffraction
2.5Å resolution

Crystal Structure of Mouse Apolipoprotein M

Released:
DOI: 10.2210/pdb2xkl/pdb
PDB entry 2xkl coloured by chain, front view.
PDB entry 2xkl coloured by chain, side view.
PDB entry 2xkl coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Mouse ApoM displays an unprecedented seven-stranded lipocalin fold: folding decoy or alternative native fold?
Sevvana M, Kassler K, Ahnström J, Weiler S, Dahlbäck B, Sticht H, Muller YA
J Mol Biol 404 363-71 (2010)
PMID: 20932978

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195540 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein M Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.1 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9Z1R3 (Residues: 20-190; Coverage: 100%)
Gene names: Apom, Ng20
Sequence domains: ApoM domain
Structure domains: Lipocalin

Ligands and Environments

4 bound ligands:
Ligand GOL 1 x GOL
Ligand POL 1 x POL
Ligand EDO 1 x EDO
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY
Spacegroup: P6522
Unit cell:
a: 53.93Å b: 53.93Å c: 207.48Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.187 0.247
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Apolipoprotein M: bridging HDL and endothelial function.
Christoffersen et al. (2013)
2 more

1 mention without citation

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