4NIF: Heterodimeric structure of ERK2 and RSK1

Heterodimeric structure of ERK2 and RSK1. Determined by X-ray diffraction at 2.15 Å resolution. Released 12 Nov 2014.

Method
X-ray diffraction
Resolution
2.15 Å
Organism
Homo sapiens
Chains
4
Atoms
11,667
Mol. weight
159.51 kDa
Ligands
ANP
Released
12 Nov 2014

Explore 4NIF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 18 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand418-427101
β-strand430-43781
β-strand442-45091
α-helix457-46610
β-strand47212
β-strand475-48061
β-strand484-49071
β-strand49612
α-helix497-5015
α-helix509-52820
β-strand531-53223
α-helix538-5403
β-strand541-54332
α-helix550-5523
β-strand553-55532
β-strand562-56323
β-strand56514
β-strand57114
α-helix583-60927
α-helix622-63110
α-helix639-6424
α-helix646-65510
α-helix660-6623
α-helix664-6652
α-helix666-6716
α-helix673-6764
α-helix678-6803
α-helix691-70616
α-helix709-7168
α-helix717-7193
α-helix721-7266
Chain B: 21 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand13-1425
β-strand17-1825
β-strand25-3396
β-strand38-4476
β-strand49-5686
α-helix62-7716
β-strand8317
β-strand88-9036
β-strand101-10666
β-strand110-11127
α-helix112-1187
α-helix120-1223
α-helix123-14220
β-strand145-14628
α-helix152-1543
β-strand155-15737
β-strand163-16537
β-strand172-17328
α-helix196-1994
α-helix208-22316
α-helix233-24412
α-helix247-2482
α-helix249-2524
α-helix259-2668
α-helix268-2692
α-helix271-2744
α-helix275-2784
α-helix284-29310
α-helix302-3032
α-helix304-3085
α-helix311-3133
α-helix319-3213
α-helix340-35112
α-helix352-3543
Chain D: 18 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand418-427109
β-strand430-43789
β-strand442-45099
α-helix457-46610
β-strand472110
β-strand475-48069
β-strand484-49079
β-strand495-496210
α-helix497-5015
α-helix509-52820
β-strand531-532211
α-helix538-5403
β-strand541-543310
α-helix550-5523
β-strand553-555310
β-strand562-563211
β-strand565112
β-strand571112
α-helix583-60927
α-helix622-63110
α-helix639-6424
α-helix646-65510
α-helix664-6652
α-helix666-6716
α-helix673-6764
α-helix678-6803
α-helix684-6874
α-helix691-70616
α-helix709-7168
α-helix717-7193
α-helix721-7266
Chain E: 22 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand13-14213
β-strand17-18213
β-strand25-33914
β-strand38-44714
β-strand49-56814
α-helix62-7716
β-strand83115
β-strand88-90314
α-helix95-973
β-strand101-106614
β-strand110-111215
α-helix112-1187
α-helix120-1223
α-helix123-14220
β-strand145-146216
α-helix152-1543
β-strand155-157315
β-strand163-165315
β-strand172-173216
α-helix196-1994
α-helix208-22316
α-helix233-24412
α-helix247-2482
α-helix249-2524
α-helix259-2668
α-helix268-2692
α-helix271-2744
α-helix275-2784
α-helix284-29310
α-helix302-3032
α-helix304-3085
α-helix311-3133
α-helix319-3213
α-helix340-35011
α-helix352-3543

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ribosomal protein S6 kinase alpha-1A, Dprotein333Homo sapiensQ15418 (AlphaFold model)
Mitogen-activated protein kinase 1B, Eprotein362Homo sapiensP28482 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>4NIF_1 Ribosomal protein S6 kinase alpha-1 (chains A, D)
GSNLVFSDGYVVKETIGVGSYSECKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQ
HPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTIGKTVEYLHS
QGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKR
QGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETA
KDLVSKMLHVDPHQRLTAKQVLQHPWVTQKDKLPQSQLSHQDLQLVKGAMAATYSALNSS
KPTPQLKPIESSILAQRRVRKLPSTTLHHHHHH
Sequence of entity 2 (B, E), FASTA
>4NIF_2 Mitogen-activated protein kinase 1 (chains B, E)
GSMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISP
FEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKT
QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH
DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLN
HILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNP
HKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGY
RS

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32

Water and common crystallization additives (NA, SO4) are not listed.

Primary citation

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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