SARS-CoV-2 S and moesin complex structure. Determined by X-ray diffraction at 1.8 Å resolution. Released 8 Oct 2025.
Explore 8XZ5 in 3D Show helices and sheets RCSB PDB PDBe
8XZ5 contains 11 α-helices and 17 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 | 5-10 | 6 | 1 |
| β-strand | 14-20 | 7 | 1 |
| β-strand | 25 | 1 | 2 |
| α-helix | 26-37 | 12 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 1 |
| β-strand | 51 | 1 | 3 |
| β-strand | 56-58 | 3 | 1 |
| β-strand | 64 | 1 | 2 |
| β-strand | 70 | 1 | 3 |
| β-strand | 76-82 | 7 | 1 |
| α-helix | 89-92 | 4 | |
| α-helix | 96-111 | 16 | |
| α-helix | 119-134 | 16 | |
| α-helix | 155-159 | 5 | |
| α-helix | 165-178 | 14 | |
| α-helix | 184-195 | 12 | |
| β-strand | 204-210 | 7 | 4 |
| β-strand | 215-221 | 7 | 4 |
| β-strand | 224-229 | 6 | 4 |
| β-strand | 236-241 | 6 | 4 |
| α-helix | 242-244 | 3 | |
| β-strand | 245-251 | 7 | 4 |
| β-strand | 254-259 | 6 | 4 |
| α-helix | 265-266 | 2 | |
| β-strand | 267-270 | 4 | 4 |
| α-helix | 274-294 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1264-1270 | 7 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Moesin | A | protein | 296 | Homo sapiens | P26038 (AlphaFold model) |
| Spike protein S2' | B | protein | 14 | Severe acute respiratory syndrome coronavirus 2 | P0DTC2 (AlphaFold model) |
>8XZ5_1 Moesin (chains A) MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLK LNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPE TAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHR GMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGF PWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRK
>8XZ5_2 Spike protein S2' (chains B) DSEPVLKGVKLHYT
SARS-CoV-2 S assembly into virions facilitated by host ERM proteins. Wang, J., Tai, W., Wang, Z. et al. Proc Natl Acad Sci U S A (2026) 123:e2504517123-e2504517123. DOI 10.1073/pnas.2504517123 · PubMed
Other PDB entries of the same protein (UniProt P26038 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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