› 1olm

X-ray diffraction
1.95Å resolution

Supernatant Protein Factor in Complex with RRR-alpha-Tocopherylquinone: A Link between Oxidized Vitamin E and Cholesterol Biosynthesis

Released:
DOI: 10.2210/pdb1olm/pdb
PDB 1olm coloured by chain and viewed from the front.
PDB 1olm coloured by chain and viewed from the side.
PDB 1olm coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Supernatant protein factor in complex with RRR-alpha-tocopherylquinone: a link between oxidized Vitamin E and cholesterol biosynthesis.
Stocker A, Baumann U
J. Mol. Biol. 332 759-65 (2003)
PMID: 12972248

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SEC14-like protein 2 Chains: A, C
Molecule details ›
Chains: A, C
Length: 403 amino acids
Theoretical weight: 46.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O76054 (Residues: 1-403; Coverage: 100%)
Gene names: C22orf6, KIAA1186, KIAA1658, SEC14L2
Structure domains:
SEC14-like protein 2 Chain: E
Molecule details ›
Chain: E
Length: 403 amino acids
Theoretical weight: 46.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O76054 (Residues: 1-403; Coverage: 100%)
Gene names: C22orf6, KIAA1186, KIAA1658, SEC14L2
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand VTQ 3 x VTQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 60.856Å b: 84.621Å c: 87.452Å
α: 116.2° β: 102.64° γ: 100.24°
R-values:
R R work R free
0.181 0.18 0.211
Expression system: Escherichia coli BL21

Quick links

Citations

12 review citations

Complexity of vitamin E metabolism.
Schmölz et al. (2016)
11 more

6 mentions without citation

Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI.
Fujita et al. (2011)
5 more