The PDZ domain of SNTG2 complexed with the phosphorylated PDZ-binding motif of RSK1. Determined by X-ray diffraction at 2.44 Å resolution. Released 20 Apr 2022.
Explore 7QQL in 3D Show helices and sheets RCSB PDB PDBe
7QQL contains 72 α-helices and 27 β-strands across 6 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 | 71-77 | 7 | 3 |
| β-strand | 79 | 1 | 4 |
| β-strand | 83 | 1 | 4 |
| β-strand | 87-89 | 3 | 3 |
| β-strand | 99-102 | 4 | 3 |
| α-helix | 108-111 | 4 | |
| β-strand | 119-124 | 6 | 3 |
| β-strand | 127-128 | 2 | 3 |
| α-helix | 134-142 | 9 | |
| β-strand | 147-154 | 8 | 3 |
| α-helix | 168-179 | 12 | |
| α-helix | 186-193 | 8 | |
| α-helix | 198-212 | 15 | |
| α-helix | 216-223 | 8 | |
| α-helix | 226-236 | 11 | |
| α-helix | 239-249 | 11 | |
| α-helix | 253-255 | 3 | |
| α-helix | 258-267 | 10 | |
| α-helix | 270-284 | 15 | |
| α-helix | 288-295 | 8 | |
| α-helix | 298-308 | 11 | |
| α-helix | 312-314 | 3 | |
| α-helix | 321-334 | 14 | |
| α-helix | 343-352 | 10 | |
| α-helix | 355-368 | 14 | |
| α-helix | 373-380 | 8 | |
| α-helix | 383-411 | 29 | |
| α-helix | 418-428 | 11 | |
| α-helix | 433-444 | 12 | |
| α-helix | 448-455 | 8 | |
| α-helix | 458-468 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 71-77 | 7 | 5 |
| β-strand | 79 | 1 | 6 |
| β-strand | 83 | 1 | 6 |
| β-strand | 86-91 | 6 | 5 |
| α-helix | 92-94 | 3 | |
| β-strand | 96-103 | 8 | 5 |
| α-helix | 108-112 | 5 | |
| β-strand | 119-124 | 6 | 5 |
| β-strand | 127-128 | 2 | 5 |
| α-helix | 134-143 | 10 | |
| β-strand | 147-154 | 8 | 5 |
| α-helix | 168-180 | 13 | |
| α-helix | 186-193 | 8 | |
| α-helix | 198-212 | 15 | |
| α-helix | 216-223 | 8 | |
| α-helix | 226-236 | 11 | |
| α-helix | 239-251 | 13 | |
| α-helix | 258-267 | 10 | |
| α-helix | 270-284 | 15 | |
| α-helix | 288-295 | 8 | |
| α-helix | 298-308 | 11 | |
| α-helix | 312-316 | 5 | |
| α-helix | 321-333 | 13 | |
| α-helix | 343-352 | 10 | |
| α-helix | 355-368 | 14 | |
| α-helix | 373-380 | 8 | |
| α-helix | 383-397 | 15 | |
| α-helix | 399-411 | 13 | |
| α-helix | 418-427 | 10 | |
| α-helix | 433-444 | 12 | |
| α-helix | 448-455 | 8 | |
| α-helix | 458-468 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 72-77 | 6 | 1 |
| α-helix | 78 | 1 | |
| β-strand | 79 | 1 | 2 |
| β-strand | 83 | 1 | 2 |
| β-strand | 86-91 | 6 | 1 |
| α-helix | 92-94 | 3 | |
| β-strand | 96-103 | 8 | 1 |
| α-helix | 108-112 | 5 | |
| α-helix | 119 | 1 | |
| β-strand | 120-124 | 5 | 1 |
| β-strand | 127-128 | 2 | 1 |
| α-helix | 134-142 | 9 | |
| β-strand | 147-153 | 7 | 1 |
| α-helix | 165-180 | 16 | |
| α-helix | 186-193 | 8 | |
| α-helix | 198-212 | 15 | |
| α-helix | 216-223 | 8 | |
| α-helix | 226-236 | 11 | |
| α-helix | 239-251 | 13 | |
| α-helix | 258-267 | 10 | |
| α-helix | 270-284 | 15 | |
| α-helix | 288-295 | 8 | |
| α-helix | 298-308 | 11 | |
| α-helix | 312-315 | 4 | |
| α-helix | 321-334 | 14 | |
| α-helix | 343-352 | 10 | |
| α-helix | 355-368 | 14 | |
| α-helix | 373-380 | 8 | |
| α-helix | 383-412 | 30 | |
| α-helix | 418-428 | 11 | |
| α-helix | 433-444 | 12 | |
| α-helix | 448-455 | 8 | |
| α-helix | 458-468 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 732-734 | 3 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gamma-2-syntrophin,Annexin A2 | A, B, C | protein | 408 | Homo sapiens | P07355 (AlphaFold model), Q9NY99 (AlphaFold model) |
| Ribosomal protein S6 kinase alpha-1 | D, E, F | protein | 11 | Homo sapiens | Q15418 (AlphaFold model) |
>7QQL_1 Gamma-2-syntrophin,Annexin A2 (chains A, B, C) GSHMGNRRTVTLRRQPVGGLGLSIKGGSEHNVPVVISKIFEDQAADQTGMLFVGDAVLQV NGIHVENATHEEVVHLLRNAGDEVTITVEYLREAPGSAYTNFDAERDALNIETAIKTKGV DEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDA SELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLM VALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDR YKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRI MVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
>7QQL_2 Ribosomal protein S6 kinase alpha-1 (chains D, E, F) RRVRKLPSTTL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 14 |
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:
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