Crystal structure of collybistin I. Determined by X-ray diffraction at 3.5 Å resolution. Released 13 Aug 2014.
Explore 4MT7 in 3D Show helices and sheets RCSB PDB PDBe
4MT7 contains 21 α-helices and 10 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 |
|---|---|---|---|
| α-helix | 50-72 | 23 | |
| α-helix | 73-77 | 5 | |
| α-helix | 78-82 | 5 | |
| α-helix | 89-96 | 8 | |
| α-helix | 99-115 | 17 | |
| α-helix | 122-124 | 3 | |
| α-helix | 128-133 | 6 | |
| α-helix | 137-139 | 3 | |
| α-helix | 140-146 | 7 | |
| α-helix | 148-158 | 11 | |
| α-helix | 162-174 | 13 | |
| α-helix | 182-185 | 4 | |
| α-helix | 188-205 | 18 | |
| α-helix | 214-232 | 19 | |
| α-helix | 233-237 | 5 | |
| α-helix | 238-250 | 13 | |
| β-strand | 252 | 1 | 1 |
| α-helix | 259-261 | 3 | |
| β-strand | 266-275 | 10 | 1 |
| α-helix | 280-282 | 3 | |
| β-strand | 283-290 | 8 | 1 |
| β-strand | 293-299 | 7 | 1 |
| β-strand | 307-314 | 8 | 1 |
| α-helix | 315-317 | 3 | |
| β-strand | 318-322 | 5 | 1 |
| α-helix | 323-324 | 2 | |
| β-strand | 326-327 | 2 | 2 |
| β-strand | 334-335 | 2 | 2 |
| β-strand | 338-343 | 6 | 1 |
| β-strand | 349-353 | 5 | 1 |
| α-helix | 357-380 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho guanine nucleotide exchange factor 9 | A | protein | 485 | Rattus norvegicus | Q9QX73 (AlphaFold model) |
>4MT7_1 Rho guanine nucleotide exchange factor 9 (chains A) MLITGDSIVSAEAVWDHVTMANRGVAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFV RLWVNQEDGVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHL KDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGP CFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTP VQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQA SVLDWEGDDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKDLIRRDILYY KGRIDMDKYEVIDIEDGRDDDFNVSMKNAFKLHNKETEEVHLFFAKKLEEKIRWLRAFRE ERKMVQEDEKIGFEISENQKRQAAMTVRKASKQKGRVGEEENQSLELKRACEVLQRLWSP GKKSC
A conformational switch in collybistin determines the differentiation of inhibitory postsynapses. Soykan, T., Schneeberger, D., Tria, G. et al. EMBO J (2014) 33:2113-2133. DOI 10.15252/embj.201488143 · PubMed
Other PDB entries of the same protein (UniProt Q9QX73 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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