› 4m91

X-ray diffraction
1.1Å resolution

crystal structure of hN33/Tusc3-peptide 1

Released:
DOI: 10.2210/pdb4m91/pdb
PDB entry 4m91 coloured by chain, front view.
PDB entry 4m91 coloured by chain, side view.
PDB entry 4m91 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of substrate specificity of human oligosaccharyl transferase subunit N33/Tusc3 and its role in regulating protein N-glycosylation.
Mohorko E, Owen RL, Malojčić G, Brozzo MS, Aebi M, Glockshuber R
Structure 22 590-601 (2014)
PMID: 24685145

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171697 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tumor suppressor candidate 3 Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 19.13 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
Protein cereblon Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96SW2 (Residues: 229-240; Coverage: 3%)
Gene names: AD-006, CRBN

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 39.769Å b: 62.235Å c: 64.551Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.138 0.137 0.16
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

2 mentions without citation

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