MAGI-1 complexed with a RSK1 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 8 Nov 2017.
Explore 5N7D in 3D Show helices and sheets RCSB PDB PDBe
5N7D contains 49 α-helices and 17 β-strands across 3 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 | 463-465 | 3 | |
| β-strand | 469-476 | 8 | 1 |
| β-strand | 478 | 1 | 2 |
| β-strand | 481 | 1 | 2 |
| β-strand | 484-487 | 4 | 1 |
| β-strand | 497-501 | 5 | 1 |
| α-helix | 506-510 | 5 | |
| β-strand | 518-522 | 5 | 1 |
| β-strand | 525-526 | 2 | 1 |
| α-helix | 532-541 | 10 | |
| α-helix | 543 | 1 | |
| β-strand | 547-554 | 8 | 1 |
| α-helix | 574-586 | 13 | |
| α-helix | 592-599 | 8 | |
| α-helix | 604-618 | 15 | |
| α-helix | 622-629 | 8 | |
| α-helix | 632-642 | 11 | |
| α-helix | 645-656 | 12 | |
| α-helix | 664-673 | 10 | |
| α-helix | 676-690 | 15 | |
| α-helix | 694-701 | 8 | |
| α-helix | 704-714 | 11 | |
| α-helix | 718-722 | 5 | |
| α-helix | 727-740 | 14 | |
| α-helix | 749-758 | 10 | |
| α-helix | 761-774 | 14 | |
| α-helix | 779-786 | 8 | |
| α-helix | 789-818 | 30 | |
| α-helix | 824-834 | 11 | |
| α-helix | 839-850 | 12 | |
| α-helix | 854-861 | 8 | |
| α-helix | 864-874 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 469 | 1 | |
| β-strand | 470-476 | 7 | 3 |
| β-strand | 484 | 1 | 4 |
| β-strand | 497 | 1 | 5 |
| β-strand | 501 | 1 | 4 |
| α-helix | 506-509 | 4 | |
| β-strand | 518 | 1 | 5 |
| β-strand | 521-522 | 2 | 3 |
| β-strand | 526 | 1 | 3 |
| α-helix | 536-541 | 6 | |
| α-helix | 543 | 1 | |
| β-strand | 547-553 | 7 | 3 |
| α-helix | 567-569 | 3 | |
| α-helix | 574-585 | 12 | |
| α-helix | 592-599 | 8 | |
| α-helix | 604-618 | 15 | |
| α-helix | 622-627 | 6 | |
| α-helix | 632-642 | 11 | |
| α-helix | 645-657 | 13 | |
| α-helix | 665-673 | 9 | |
| α-helix | 676-690 | 15 | |
| α-helix | 694-701 | 8 | |
| α-helix | 704-714 | 11 | |
| α-helix | 718-720 | 3 | |
| α-helix | 727-740 | 14 | |
| α-helix | 749-758 | 10 | |
| α-helix | 761-774 | 14 | |
| α-helix | 779-786 | 8 | |
| α-helix | 789-818 | 30 | |
| α-helix | 824-834 | 11 | |
| α-helix | 839-850 | 12 | |
| α-helix | 854-861 | 8 | |
| α-helix | 865-874 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 733-734 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1,Annexin A2 | A, B | protein | 427 | Homo sapiens | P07355 (AlphaFold model), Q96QZ7 (AlphaFold model) |
| Ribosomal protein S6 kinase alpha-1 | C | protein | 49 | Homo sapiens | Q15418 (AlphaFold model) |
>5N7D_1 Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1,Annexin A2 (chains A, B) GSMGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDG KMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLGSSAYGSVKAYTN FDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALS GHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYK TDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPK WISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFAD RLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALL YLCGGDD
>5N7D_2 Ribosomal protein S6 kinase alpha-1 (chains C) GSQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 7 |
Water and common crystallization additives (GOL) are not listed.
Dynamic control of RSK complexes by phosphoswitch-based regulation. Gogl, G., Biri-Kovacs, B., Poti, A.L. et al. FEBS J (2018) 285:46-71. DOI 10.1111/febs.14311 · 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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