MAGI-1 complexed with a pRSK1 peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 8 Nov 2017.
Explore 5N7F in 3D Show helices and sheets RCSB PDB PDBe
5N7F contains 47 α-helices and 18 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 | 478-482 | 5 | 2 |
| β-strand | 484-488 | 5 | 1 |
| β-strand | 496-501 | 6 | 1 |
| α-helix | 506-510 | 5 | |
| β-strand | 518-522 | 5 | 1 |
| β-strand | 525-526 | 2 | 1 |
| α-helix | 532-540 | 9 | |
| 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 | 718-720 | 3 | |
| α-helix | 727-739 | 13 | |
| α-helix | 749-758 | 10 | |
| α-helix | 761-774 | 14 | |
| α-helix | 779-786 | 8 | |
| α-helix | 789-803 | 15 | |
| α-helix | 805-817 | 13 | |
| α-helix | 824-834 | 11 | |
| α-helix | 839-850 | 12 | |
| α-helix | 854-861 | 8 | |
| α-helix | 864-874 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 469-473 | 5 | 3 |
| β-strand | 476 | 1 | 4 |
| β-strand | 478 | 1 | 5 |
| β-strand | 481 | 1 | 5 |
| β-strand | 486-488 | 3 | 3 |
| β-strand | 496-498 | 3 | 3 |
| β-strand | 518-522 | 5 | 3 |
| β-strand | 525-526 | 2 | 3 |
| α-helix | 534-540 | 7 | |
| β-strand | 547 | 1 | 4 |
| β-strand | 550-554 | 5 | 3 |
| α-helix | 574-586 | 13 | |
| α-helix | 592-599 | 8 | |
| α-helix | 604-618 | 15 | |
| α-helix | 622-627 | 6 | |
| α-helix | 632-641 | 10 | |
| α-helix | 645-656 | 12 | |
| α-helix | 664-673 | 10 | |
| α-helix | 676-690 | 15 | |
| α-helix | 694-701 | 8 | |
| α-helix | 705-714 | 10 | |
| 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 | 789-803 | 15 | |
| α-helix | 805-818 | 14 | |
| α-helix | 824-834 | 11 | |
| α-helix | 839-850 | 12 | |
| α-helix | 854-861 | 8 | |
| α-helix | 864-874 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 732-734 | 3 | 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) |
>5N7F_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
>5N7F_2 Ribosomal protein S6 kinase alpha-1 (chains C) GSQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 9 |
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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