Crystal structure of Se-Met hN33/Tusc3. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Mar 2014.
Explore 4M8G in 3D Show helices and sheets RCSB PDB PDBe
4M8G contains 18 α-helices and 10 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 25-27 | 3 | 1 |
| α-helix | 29-32 | 4 | |
| α-helix | 33-37 | 5 | |
| α-helix | 40 | 1 | |
| β-strand | 44-50 | 7 | 1 |
| α-helix | 54-56 | 3 | |
| α-helix | 59-77 | 19 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 96-101 | 6 | |
| β-strand | 109-113 | 5 | 1 |
| α-helix | 121-123 | 3 | |
| β-strand | 124 | 1 | 1 |
| α-helix | 127-130 | 4 | |
| α-helix | 134-145 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tumor suppressor candidate 3 | A, B | protein | 161 | Homo sapiens | Q13454 (AlphaFold model) |
>4M8G_1 Tumor suppressor candidate 3 (chains A, B) ASKKENLLAEKVEQLMEWSSRRSIFRMNGDKFRKFIKAPPRNYSMIVMFTALQPQRQCSV CRQANEEYQILANSWRYSSAFSNKLFFSMVDYDEGTDVFQQLNMNSAPTFMHFPPKGRPK RADTFDLQRIGFAAEQLAKWIADRTDVHIRVFRLEHHHHHH
Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation. Mohorko, E., Owen, R.L., Malojcic, G. et al. Structure (2014) 22:590-601. DOI 10.1016/j.str.2014.02.013 · PubMed
Other PDB entries of the same protein (UniProt Q13454 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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