Crystal structure of human ERK2 complexed with a MAPK docking peptide. Determined by X-ray diffraction at 2.4 Å resolution. Released 15 Aug 2012.
Explore 3TEI in 3D Show helices and sheets RCSB PDB PDBe
3TEI contains 20 α-helices and 13 β-strands across 2 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 | 12-14 | 3 | 1 |
| β-strand | 17-19 | 3 | 1 |
| β-strand | 25-33 | 9 | 2 |
| β-strand | 38-44 | 7 | 2 |
| β-strand | 49-56 | 8 | 2 |
| α-helix | 62-77 | 16 | |
| β-strand | 83 | 1 | 3 |
| β-strand | 88-90 | 3 | 2 |
| β-strand | 101-106 | 6 | 2 |
| α-helix | 107-108 | 2 | |
| β-strand | 110-111 | 2 | 3 |
| α-helix | 112-118 | 7 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-142 | 20 | |
| β-strand | 145-146 | 2 | 4 |
| α-helix | 152-154 | 3 | |
| β-strand | 155-157 | 3 | 3 |
| β-strand | 163-165 | 3 | 3 |
| β-strand | 172-173 | 2 | 4 |
| α-helix | 196-200 | 5 | |
| α-helix | 208-223 | 16 | |
| α-helix | 233-244 | 12 | |
| α-helix | 259-265 | 7 | |
| α-helix | 268-269 | 2 | |
| α-helix | 271-274 | 4 | |
| α-helix | 284-293 | 10 | |
| α-helix | 302-303 | 2 | |
| α-helix | 304-308 | 5 | |
| α-helix | 311-313 | 3 | |
| α-helix | 340-350 | 11 | |
| α-helix | 352-354 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 717-719 | 3 | |
| α-helix | 721-726 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 1 | A | protein | 362 | Homo sapiens | P28482 (AlphaFold model) |
| Ribosomal protein S6 kinase alpha-1 | B | protein | 24 | Homo sapiens | Q15418 (AlphaFold model) |
>3TEI_1 Mitogen-activated protein kinase 1 (chains A) GSMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISP FEHQTYCQRTLREIKILLAFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKT QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLN HILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNP HKRIEVEQALAHPYLAQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGY RS
>3TEI_2 Ribosomal protein S6 kinase alpha-1 (chains B) PQLKPIESSILAQRRVRKLPSTTL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking groove. Garai, A., Zeke, A., Gogl, G. et al. Sci Signal (2012) 5:ra74-ra74. DOI 10.1126/scisignal.2003004 · 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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