The PDZ domain of SNTG1 complexed with the phosphomimetic mutant PDZ-binding motif of RSK1. Determined by X-ray diffraction at 2.5 Å resolution. Released 20 Apr 2022.
Explore 7PC8 in 3D Show helices and sheets RCSB PDB PDBe
7PC8 contains 49 α-helices and 18 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 |
|---|---|---|---|
| β-strand | 51-52 | 2 | 1 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-61 | 6 | 2 |
| β-strand | 63 | 1 | 3 |
| β-strand | 67 | 1 | 3 |
| β-strand | 70-75 | 6 | 2 |
| α-helix | 76-78 | 3 | |
| β-strand | 80-87 | 8 | 2 |
| α-helix | 89-94 | 6 | |
| β-strand | 103-108 | 6 | 2 |
| β-strand | 111-112 | 2 | 2 |
| α-helix | 118-126 | 9 | |
| β-strand | 131-138 | 8 | 2 |
| β-strand | 139-140 | 2 | 1 |
| α-helix | 141-143 | 3 | |
| α-helix | 158-170 | 13 | |
| α-helix | 176-183 | 8 | |
| α-helix | 188-202 | 15 | |
| α-helix | 206-213 | 8 | |
| α-helix | 216-226 | 11 | |
| α-helix | 229-240 | 12 | |
| α-helix | 248-257 | 10 | |
| α-helix | 260-274 | 15 | |
| α-helix | 278-285 | 8 | |
| α-helix | 288-298 | 11 | |
| α-helix | 302-306 | 5 | |
| α-helix | 311-324 | 14 | |
| α-helix | 333-342 | 10 | |
| α-helix | 345-358 | 14 | |
| α-helix | 363-370 | 8 | |
| α-helix | 373-387 | 15 | |
| α-helix | 389-402 | 14 | |
| α-helix | 408-417 | 10 | |
| α-helix | 423-434 | 12 | |
| α-helix | 438-445 | 8 | |
| α-helix | 448-458 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 55-61 | 7 | 4 |
| β-strand | 70-75 | 6 | 4 |
| α-helix | 76-78 | 3 | |
| β-strand | 80-87 | 8 | 4 |
| α-helix | 89-95 | 7 | |
| β-strand | 103-108 | 6 | 4 |
| β-strand | 111-112 | 2 | 4 |
| α-helix | 118-126 | 9 | |
| β-strand | 131-138 | 8 | 4 |
| α-helix | 158-170 | 13 | |
| α-helix | 176-183 | 8 | |
| α-helix | 188-202 | 15 | |
| α-helix | 206-213 | 8 | |
| α-helix | 216-226 | 11 | |
| α-helix | 229-240 | 12 | |
| α-helix | 248-257 | 10 | |
| α-helix | 260-274 | 15 | |
| α-helix | 278-285 | 8 | |
| α-helix | 288-298 | 11 | |
| α-helix | 302-304 | 3 | |
| α-helix | 311-323 | 13 | |
| α-helix | 333-342 | 10 | |
| α-helix | 345-358 | 14 | |
| α-helix | 363-370 | 8 | |
| α-helix | 373-401 | 29 | |
| α-helix | 408-417 | 10 | |
| α-helix | 423-434 | 12 | |
| α-helix | 438-445 | 8 | |
| α-helix | 448-458 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 186-188 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gamma-1-syntrophin,Annexin A2 | A, B | protein | 414 | Homo sapiens | P07355 (AlphaFold model), Q9NSN8 (AlphaFold model) |
| Ribosomal protein S6 kinase alpha-1 | C, D | protein | 10 | Homo sapiens | Q15418 (AlphaFold model) |
>7PC8_1 Gamma-1-syntrophin,Annexin A2 (chains A, B) GSHMGGERTVTIRRQTVGGFGLSIKGGAEHNIPVVVSKISKEQRAELSGLLFIGDAILQI NGINVRKCRHEEVVQVLRNAGEEVTLTVSFLKRAPGSAYGSVKAYTNFDAERDALNIETA IKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKT PAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSG DFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHL QKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRD KVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
>7PC8_2 Ribosomal protein S6 kinase alpha-1 (chains C, D) RVRKLPETTL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 9 |
Water and common crystallization additives (GOL) are not listed.
A scalable strategy to solve structures of PDZ domains and their complexes. Cousido-Siah, A., Carneiro, L., Kostmann, C. et al. Acta Crystallogr D Struct Biol (2022) 78:509-516. DOI 10.1107/S2059798322001784 · PubMed
Other PDB entries of the same protein (UniProt P07355 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7PC8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.