Structure of SCGN in complex with a Snap25 peptide. Determined by X-ray diffraction at 2.37 Å resolution. Released 11 Mar 2020.
Explore 6JLH in 3D Show helices and sheets RCSB PDB PDBe
6JLH contains 34 α-helices and 12 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 | 10-20 | 11 | |
| β-strand | 28 | 1 | 1 |
| α-helix | 31-44 | 14 | |
| α-helix | 49-50 | 2 | |
| α-helix | 52-66 | 15 | |
| β-strand | 74 | 1 | 1 |
| α-helix | 76-83 | 8 | |
| α-helix | 86-88 | 3 | |
| α-helix | 90-94 | 5 | |
| α-helix | 103-113 | 11 | |
| β-strand | 121 | 1 | 2 |
| α-helix | 123-136 | 14 | |
| α-helix | 143-157 | 15 | |
| β-strand | 165 | 1 | 2 |
| α-helix | 167-173 | 7 | |
| α-helix | 180-183 | 4 | |
| α-helix | 191-205 | 15 | |
| β-strand | 212-213 | 2 | 3 |
| α-helix | 216-226 | 11 | |
| α-helix | 235-249 | 15 | |
| β-strand | 257-258 | 2 | 3 |
| α-helix | 259-266 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-16 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-20 | 8 | |
| β-strand | 28 | 1 | 4 |
| α-helix | 31-44 | 14 | |
| α-helix | 49-50 | 2 | |
| α-helix | 52-66 | 15 | |
| β-strand | 74 | 1 | 4 |
| α-helix | 76-83 | 8 | |
| α-helix | 84-86 | 3 | |
| α-helix | 88-92 | 5 | |
| α-helix | 103-113 | 11 | |
| β-strand | 121 | 1 | 5 |
| α-helix | 123-136 | 14 | |
| α-helix | 143-157 | 15 | |
| β-strand | 165 | 1 | 5 |
| α-helix | 167-173 | 7 | |
| α-helix | 181-183 | 3 | |
| α-helix | 191-205 | 15 | |
| β-strand | 212-213 | 2 | 6 |
| α-helix | 216-226 | 11 | |
| α-helix | 235-249 | 15 | |
| β-strand | 257-258 | 2 | 6 |
| α-helix | 259-266 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-14 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Secretagogin | A, C | protein | 261 | Danio rerio | Q5XJX1 (AlphaFold model) |
| Synaptosomal-associated protein 25 | B, D | protein | 17 | Homo sapiens | P60880 (AlphaFold model) |
>6JLH_1 Secretagogin (chains A, C) NLDAAGFLQIWQHFDADDNGYIEGKELDDFFRHMLKKLQPKDKITDERVQQIKKSFMSAY DATFDGRLQIEELANMILPQEENFLLIFRREAPLDNSVEFMKIWRKYDADSSGYISAAEL KNFLKDLFLQHKKKIPPNKLDEYTDAMMKIFDKNKDGRLDLNDLARILALQENFLLQFKM DASSQVERKRDFEKIFAHYDVSRTGALEGPEVDGFVKDMMELVRPSISGGDLDKFRECLL THCDMNKDGKIQKSELALCLG
>6JLH_2 Synaptosomal-associated protein 25 (chains B, D) SGIIGNLRHMALDMGNE
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 12 |
Water and common crystallization additives (CL) are not listed.
Structural and mechanistic insights into secretagogin-mediated exocytosis. Qin, J., Liu, Q., Liu, Z. et al. Proc Natl Acad Sci U S A (2020) 117:6559-6570. DOI 10.1073/pnas.1919698117 · PubMed
Other PDB entries of the same protein (UniProt Q5XJX1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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