Heterodimeric structure of ERK2 and RSK1. Determined by X-ray diffraction at 2.15 Å resolution. Released 12 Nov 2014.
Explore 4NIF in 3D Show helices and sheets RCSB PDB PDBe
4NIF contains 79 α-helices and 52 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 | 418-427 | 10 | 1 |
| β-strand | 430-437 | 8 | 1 |
| β-strand | 442-450 | 9 | 1 |
| α-helix | 457-466 | 10 | |
| β-strand | 472 | 1 | 2 |
| β-strand | 475-480 | 6 | 1 |
| β-strand | 484-490 | 7 | 1 |
| β-strand | 496 | 1 | 2 |
| α-helix | 497-501 | 5 | |
| α-helix | 509-528 | 20 | |
| β-strand | 531-532 | 2 | 3 |
| α-helix | 538-540 | 3 | |
| β-strand | 541-543 | 3 | 2 |
| α-helix | 550-552 | 3 | |
| β-strand | 553-555 | 3 | 2 |
| β-strand | 562-563 | 2 | 3 |
| β-strand | 565 | 1 | 4 |
| β-strand | 571 | 1 | 4 |
| α-helix | 583-609 | 27 | |
| α-helix | 622-631 | 10 | |
| α-helix | 639-642 | 4 | |
| α-helix | 646-655 | 10 | |
| α-helix | 660-662 | 3 | |
| α-helix | 664-665 | 2 | |
| α-helix | 666-671 | 6 | |
| α-helix | 673-676 | 4 | |
| α-helix | 678-680 | 3 | |
| α-helix | 691-706 | 16 | |
| α-helix | 709-716 | 8 | |
| α-helix | 717-719 | 3 | |
| α-helix | 721-726 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-14 | 2 | 5 |
| β-strand | 17-18 | 2 | 5 |
| β-strand | 25-33 | 9 | 6 |
| β-strand | 38-44 | 7 | 6 |
| β-strand | 49-56 | 8 | 6 |
| α-helix | 62-77 | 16 | |
| β-strand | 83 | 1 | 7 |
| β-strand | 88-90 | 3 | 6 |
| β-strand | 101-106 | 6 | 6 |
| β-strand | 110-111 | 2 | 7 |
| α-helix | 112-118 | 7 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-142 | 20 | |
| β-strand | 145-146 | 2 | 8 |
| α-helix | 152-154 | 3 | |
| β-strand | 155-157 | 3 | 7 |
| β-strand | 163-165 | 3 | 7 |
| β-strand | 172-173 | 2 | 8 |
| α-helix | 196-199 | 4 | |
| α-helix | 208-223 | 16 | |
| α-helix | 233-244 | 12 | |
| α-helix | 247-248 | 2 | |
| α-helix | 249-252 | 4 | |
| α-helix | 259-266 | 8 | |
| α-helix | 268-269 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 275-278 | 4 | |
| α-helix | 284-293 | 10 | |
| α-helix | 302-303 | 2 | |
| α-helix | 304-308 | 5 | |
| α-helix | 311-313 | 3 | |
| α-helix | 319-321 | 3 | |
| α-helix | 340-351 | 12 | |
| α-helix | 352-354 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 418-427 | 10 | 9 |
| β-strand | 430-437 | 8 | 9 |
| β-strand | 442-450 | 9 | 9 |
| α-helix | 457-466 | 10 | |
| β-strand | 472 | 1 | 10 |
| β-strand | 475-480 | 6 | 9 |
| β-strand | 484-490 | 7 | 9 |
| β-strand | 495-496 | 2 | 10 |
| α-helix | 497-501 | 5 | |
| α-helix | 509-528 | 20 | |
| β-strand | 531-532 | 2 | 11 |
| α-helix | 538-540 | 3 | |
| β-strand | 541-543 | 3 | 10 |
| α-helix | 550-552 | 3 | |
| β-strand | 553-555 | 3 | 10 |
| β-strand | 562-563 | 2 | 11 |
| β-strand | 565 | 1 | 12 |
| β-strand | 571 | 1 | 12 |
| α-helix | 583-609 | 27 | |
| α-helix | 622-631 | 10 | |
| α-helix | 639-642 | 4 | |
| α-helix | 646-655 | 10 | |
| α-helix | 664-665 | 2 | |
| α-helix | 666-671 | 6 | |
| α-helix | 673-676 | 4 | |
| α-helix | 678-680 | 3 | |
| α-helix | 684-687 | 4 | |
| α-helix | 691-706 | 16 | |
| α-helix | 709-716 | 8 | |
| α-helix | 717-719 | 3 | |
| α-helix | 721-726 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 13-14 | 2 | 13 |
| β-strand | 17-18 | 2 | 13 |
| β-strand | 25-33 | 9 | 14 |
| β-strand | 38-44 | 7 | 14 |
| β-strand | 49-56 | 8 | 14 |
| α-helix | 62-77 | 16 | |
| β-strand | 83 | 1 | 15 |
| β-strand | 88-90 | 3 | 14 |
| α-helix | 95-97 | 3 | |
| β-strand | 101-106 | 6 | 14 |
| β-strand | 110-111 | 2 | 15 |
| α-helix | 112-118 | 7 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-142 | 20 | |
| β-strand | 145-146 | 2 | 16 |
| α-helix | 152-154 | 3 | |
| β-strand | 155-157 | 3 | 15 |
| β-strand | 163-165 | 3 | 15 |
| β-strand | 172-173 | 2 | 16 |
| α-helix | 196-199 | 4 | |
| α-helix | 208-223 | 16 | |
| α-helix | 233-244 | 12 | |
| α-helix | 247-248 | 2 | |
| α-helix | 249-252 | 4 | |
| α-helix | 259-266 | 8 | |
| α-helix | 268-269 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 275-278 | 4 | |
| α-helix | 284-293 | 10 | |
| α-helix | 302-303 | 2 | |
| α-helix | 304-308 | 5 | |
| α-helix | 311-313 | 3 | |
| α-helix | 319-321 | 3 | |
| α-helix | 340-350 | 11 | |
| α-helix | 352-354 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribosomal protein S6 kinase alpha-1 | A, D | protein | 333 | Homo sapiens | Q15418 (AlphaFold model) |
| Mitogen-activated protein kinase 1 | B, E | protein | 362 | Homo sapiens | P28482 (AlphaFold model) |
>4NIF_1 Ribosomal protein S6 kinase alpha-1 (chains A, D) GSNLVFSDGYVVKETIGVGSYSECKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQ HPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTIGKTVEYLHS QGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKR QGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETA KDLVSKMLHVDPHQRLTAKQVLQHPWVTQKDKLPQSQLSHQDLQLVKGAMAATYSALNSS KPTPQLKPIESSILAQRRVRKLPSTTLHHHHHH
>4NIF_2 Mitogen-activated protein kinase 1 (chains B, E) GSMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISP FEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKT QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLN HILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNP HKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGY RS
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Water and common crystallization additives (NA, SO4) are not listed.
Structural assembly of the signaling competent ERK2-RSK1 heterodimeric protein kinase complex. Alexa, A., Gogl, G., Glatz, G. et al. Proc Natl Acad Sci U S A (2015) 112:2711-2716. DOI 10.1073/pnas.1417571112 · PubMed
Other PDB entries of the same protein (UniProt Q15418 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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