4H3P: Human ERK2

Crystal structure of human ERK2 complexed with a MAPK docking peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Feb 2013.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
4
Atoms
5,926
Mol. weight
89.23 kDa
Ligands
ANP
Released
27 Feb 2013

Explore 4H3P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4H3P contains 45 α-helices and 26 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: 19 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand12-1431
β-strand17-1931
β-strand25-3392
β-strand37-4482
β-strand49-5682
α-helix62-7716
β-strand8313
β-strand88-9032
β-strand101-10662
β-strand110-11123
α-helix112-1165
α-helix120-1223
α-helix123-14220
β-strand145-14624
α-helix152-1543
β-strand155-15733
β-strand163-16533
β-strand172-17324
α-helix196-1983
α-helix208-22316
α-helix233-24412
α-helix247-2482
α-helix261-2655
α-helix268-2692
α-helix284-29310
α-helix298-3003
α-helix302-3032
α-helix304-3085
α-helix311-3133
α-helix319-3213
α-helix340-35112
α-helix352-3543
Chains B and E: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix717-7193
α-helix721-7244
Chain D: 22 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand12-1435
β-strand17-1935
β-strand25-3396
β-strand37-4486
β-strand49-5686
α-helix62-7716
β-strand8317
β-strand88-9036
β-strand101-10666
α-helix107-1082
β-strand110-11127
α-helix112-1154
α-helix120-1223
α-helix123-14220
β-strand145-14628
α-helix152-1543
β-strand155-15737
β-strand163-16537
β-strand172-17328
α-helix191-1933
α-helix196-2005
α-helix208-22316
α-helix233-24412
α-helix247-2482
α-helix262-2665
α-helix268-2692
α-helix271-2744
α-helix284-29310
α-helix298-3003
α-helix302-3032
α-helix304-3085
α-helix311-3133
α-helix319-3213
α-helix340-35011
α-helix352-3543

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mitogen-activated protein kinase 1A, Dprotein362Homo sapiensP28482 (AlphaFold model)
Ribosomal protein S6 kinase alpha-1B, Eprotein24Homo sapiensQ15418 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>4H3P_1 Mitogen-activated protein kinase 1 (chains A, D)
GSMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISP
FEHQTYCQRTLREIKILLAFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKT
QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH
DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLN
HILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNP
HKRIEVEQALAHPYLAQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGY
RS
Sequence of entity 2 (B, E), FASTA
>4H3P_2 Ribosomal protein S6 kinase alpha-1 (chains B, E)
PQLKPIEASILAARRVRKLPSTTL

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32

Primary citation

Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase. Gogl, G., Toeroe, I., Remenyi, A. Acta Crystallogr D Biol Crystallogr (2013) 69:486-489. DOI 10.1107/S0907444912051062 · PubMed

Other PDB entries of the same protein (UniProt P28482 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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