Moesin FERM domain bound to EBP50 C-terminal peptide. Determined by X-ray diffraction at 3.5 Å resolution. Released 29 Jun 2004.
Explore 1SGH in 3D Show helices and sheets RCSB PDB PDBe
1SGH contains 8 α-helices and 16 β-strands across 1 chain. 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 | 7-10 | 4 | 1 |
| β-strand | 15-18 | 4 | 1 |
| β-strand | 25 | 1 | 2 |
| α-helix | 26-36 | 11 | |
| 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 | 98-110 | 13 | |
| α-helix | 119-131 | 13 | |
| α-helix | 155-158 | 4 | |
| α-helix | 165-177 | 13 | |
| α-helix | 186-195 | 10 | |
| β-strand | 204-209 | 6 | 4 |
| β-strand | 215-221 | 7 | 4 |
| β-strand | 224-228 | 5 | 4 |
| β-strand | 238-241 | 4 | 4 |
| β-strand | 247-251 | 5 | 4 |
| β-strand | 254-258 | 5 | 4 |
| β-strand | 267-270 | 4 | 4 |
| α-helix | 274-295 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Moesin | A | protein | 297 | Homo sapiens | P26038 (AlphaFold model) |
| Ezrin-radixin-moesin binding phosphoprotein 50 | B | protein | 39 | O14745 (AlphaFold model) |
>1SGH_1 Moesin (chains A) MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLK LNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPE TAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHR GMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGF PWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKP
>1SGH_2 Ezrin-radixin-moesin binding phosphoprotein 50 (chains B) CLDFNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL
The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain. Finnerty, C.M., Chambers, D., Ingraffea, J. et al. J Cell Sci (2004) 117:1547-1552. DOI 10.1242/jcs.01038 · 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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