› 3ga4

X-ray diffraction
1.3Å resolution

Crystal structure of Ost6L (photoreduced form)

Released:
DOI: 10.2210/pdb3ga4/pdb
PDB entry 3ga4 coloured by chain, front view.
PDB entry 3ga4 coloured by chain, side view.
PDB entry 3ga4 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency.
Schulz BL, Stirnimann CU, Grimshaw JP, Brozzo MS, Fritsch F, Mohorko E, Capitani G, Glockshuber R, Grütter MG, Aebi M
Proc Natl Acad Sci U S A 106 11061-6 (2009)
PMID: 19549845

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169941 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6 Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.34 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03723 (Residues: 24-188; Coverage: 53%)
Gene names: OST6, YML019W
Sequence domains: OST3 / OST6 family, transporter family
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand PG4 1 x PG4
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I222
Unit cell:
a: 58.989Å b: 61.076Å c: 106.985Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.187
Expression system: Escherichia coli

Quick links

Citations

26 review citations

Protein folding and modification in the mammalian endoplasmic reticulum.
Braakman et al. (2011)
25 more

2 mentions without citation

Structural Insight into the Mechanism of N-Linked Glycosylation by Oligosaccharyltransferase.
Mohanty et al. (2020)
1 more