Crystal structure of BST2/Tetherin. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Jul 2010.
Explore 3NWH in 3D Show helices and sheets RCSB PDB PDBe
3NWH contains 5 α-helices and 0 β-strands across 4 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 |
|---|---|---|---|
| α-helix | 51-149 | 99 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 49-111 | 63 | |
| α-helix | 116-149 | 34 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 49-150 | 102 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bone marrow stromal antigen 2 | A, B, C, D | protein | 112 | Homo sapiens | Q10589 (AlphaFold model) |
>3NWH_1 Bone marrow stromal antigen 2 (chains A, B, C, D) GIDPFTKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMA SLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKK
Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations. Schubert, H.L., Zhai, Q., Sandrin, V. et al. Proc Natl Acad Sci U S A (2010) 107:17951-17956. DOI 10.1073/pnas.1008206107 · PubMed
Other PDB entries of the same protein (UniProt Q10589 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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