› 4m8g

X-ray diffraction
2Å resolution

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-171696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tumor suppressor candidate 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 161 amino acids
Theoretical weight: 19.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13454 (Residues: 44-194; Coverage: 49%)
Gene names: N33, TUSC3
Sequence domains: OST3 / OST6 family, transporter family

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 39.107Å b: 64.456Å c: 62.467Å
α: 90° β: 92.45° γ: 90°
R-values:
R R work R free
0.229 0.229 0.248
Expression system: Escherichia coli

Quick links

Citations

17 review citations

N-linked sugar-regulated protein folding and quality control in the ER.
Tannous et al. (2015)
16 more

1 mention without citation

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