Regulation of protein interactions by MOB1 phosphorylation. Determined by X-ray diffraction at 3.14 Å resolution. Released 12 Apr 2017.
Explore 5TWF in 3D Show helices and sheets RCSB PDB PDBe
5TWF contains 24 α-helices and 8 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 |
|---|---|---|---|
| α-helix | 25-34 | 10 | |
| α-helix | 35-38 | 4 | |
| α-helix | 41-44 | 4 | |
| α-helix | 47-48 | 2 | |
| α-helix | 53-74 | 22 | |
| α-helix | 76-78 | 3 | |
| β-strand | 87-88 | 2 | 1 |
| β-strand | 94-95 | 2 | 1 |
| β-strand | 97 | 1 | 2 |
| β-strand | 107 | 1 | 2 |
| α-helix | 111-126 | 16 | |
| α-helix | 139-141 | 3 | |
| α-helix | 146-164 | 19 | |
| α-helix | 167-171 | 5 | |
| α-helix | 177-193 | 17 | |
| α-helix | 205-210 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-34 | 11 | |
| α-helix | 35-38 | 4 | |
| α-helix | 47-48 | 2 | |
| α-helix | 53-74 | 22 | |
| β-strand | 88 | 1 | 3 |
| β-strand | 94 | 1 | 3 |
| β-strand | 96-97 | 2 | 4 |
| β-strand | 107-108 | 2 | 4 |
| α-helix | 111-126 | 16 | |
| α-helix | 138-141 | 4 | |
| α-helix | 144-164 | 21 | |
| α-helix | 167-172 | 6 | |
| α-helix | 177-193 | 17 | |
| α-helix | 198-201 | 4 | |
| α-helix | 202-204 | 3 | |
| α-helix | 205-208 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MOB kinase activator 1A | A, B | protein | 216 | Homo sapiens | Q9H8S9 (AlphaFold model) |
>5TWF_1 MOB kinase activator 1A (chains A, B) MSFLFSSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRQAVMLPEGEDLNEWIAVN TVDFFNQINMLYGTITEFCTEASCPVMSAGPRYEYHWADGTNIKKPIKCSAPKYIDYLMT WVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDSVMQLEEEAHLN TSFKHFIFFVQEFNLIDRRELAPLQELIEKLGSKDR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Regulation of Protein Interactions by Mps One Binder (MOB1) Phosphorylation. Xiong, S., Couzens, A.L., Kean, M.J. et al. Mol Cell Proteomics (2017) 16:1111-1125. DOI 10.1074/mcp.M117.068130 · PubMed
Other PDB entries of the same protein (UniProt Q9H8S9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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