The PDZ domain of SNTG1 complexed with the acetylated PDZ-binding motif of PTEN. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 Apr 2022.
Explore 7PC7 in 3D Show helices and sheets RCSB PDB PDBe
7PC7 contains 49 α-helices and 15 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 | 56-61 | 6 | 1 |
| β-strand | 70-73 | 4 | 1 |
| α-helix | 76-78 | 3 | |
| α-helix | 81-82 | 2 | |
| β-strand | 83-87 | 5 | 1 |
| α-helix | 89-94 | 6 | |
| β-strand | 96 | 1 | 1 |
| β-strand | 103-108 | 6 | 1 |
| β-strand | 111-112 | 2 | 1 |
| α-helix | 118-126 | 9 | |
| β-strand | 131-138 | 8 | 1 |
| α-helix | 157-169 | 13 | |
| α-helix | 175-182 | 8 | |
| α-helix | 187-201 | 15 | |
| α-helix | 205-212 | 8 | |
| α-helix | 215-225 | 11 | |
| α-helix | 228-240 | 13 | |
| α-helix | 247-256 | 10 | |
| α-helix | 259-273 | 15 | |
| α-helix | 277-284 | 8 | |
| α-helix | 287-297 | 11 | |
| α-helix | 301-305 | 5 | |
| α-helix | 310-323 | 14 | |
| α-helix | 332-341 | 10 | |
| α-helix | 344-357 | 14 | |
| α-helix | 362-369 | 8 | |
| α-helix | 372-400 | 29 | |
| α-helix | 407-417 | 11 | |
| α-helix | 422-433 | 12 | |
| α-helix | 437-444 | 8 | |
| α-helix | 447-457 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 56-61 | 6 | 2 |
| α-helix | 62-63 | 2 | |
| β-strand | 70-75 | 6 | 2 |
| α-helix | 76-78 | 3 | |
| β-strand | 80-87 | 8 | 2 |
| α-helix | 89-95 | 7 | |
| β-strand | 103-108 | 6 | 2 |
| β-strand | 111-112 | 2 | 2 |
| α-helix | 118-126 | 9 | |
| β-strand | 131-138 | 8 | 2 |
| α-helix | 157-169 | 13 | |
| α-helix | 175-182 | 8 | |
| α-helix | 187-201 | 15 | |
| α-helix | 205-212 | 8 | |
| α-helix | 215-225 | 11 | |
| α-helix | 228-240 | 13 | |
| α-helix | 247-256 | 10 | |
| α-helix | 259-273 | 15 | |
| α-helix | 277-284 | 8 | |
| α-helix | 287-297 | 11 | |
| α-helix | 301-304 | 4 | |
| α-helix | 310-323 | 14 | |
| α-helix | 332-341 | 10 | |
| α-helix | 344-357 | 14 | |
| α-helix | 362-369 | 8 | |
| α-helix | 372-401 | 30 | |
| α-helix | 407-417 | 11 | |
| α-helix | 422-433 | 12 | |
| α-helix | 437-444 | 8 | |
| α-helix | 447-457 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 94-96 | 3 | |
| β-strand | 97-99 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 64-65 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gamma-1-syntrophin,Annexin A2 | A, B | protein | 414 | Homo sapiens | P07355 (AlphaFold model), Q9NSN8 (AlphaFold model) |
| Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN | E, F | protein | 10 | Homo sapiens | P60484 (AlphaFold model) |
>7PC7_1 Gamma-1-syntrophin,Annexin A2 (chains A, B) GSHMGGERTVTIRRQTVGGFGLSIKGGAEHNIPVVVSKISKEQRAELSGLLFIGDAILQI NGINVRKCRHEEVVQVLRNAGEEVTLTVSFLKRAPGSAYGSVKAYTNFDAERDALNIETA IKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKT PAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSG DFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHL QKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRD KVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
>7PC7_2 Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (chains E, F) EDQHTQITKV
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 12 |
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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