Crystal structure of the MAPK binding domain of MKP7. Determined by X-ray diffraction at 2.67 Å resolution. Released 14 Mar 2012.
Explore 3TG3 in 3D Show helices and sheets RCSB PDB PDBe
3TG3 contains 28 α-helices and 28 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 | 9-10 | 2 | 1 |
| α-helix | 12-20 | 9 | |
| β-strand | 26-30 | 5 | 1 |
| α-helix | 34-39 | 6 | |
| β-strand | 41-42 | 2 | 2 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 52-60 | 9 | |
| α-helix | 65-72 | 8 | |
| β-strand | 84-88 | 5 | 1 |
| α-helix | 103-112 | 10 | |
| β-strand | 118-121 | 4 | 1 |
| α-helix | 124-131 | 8 | |
| α-helix | 133-135 | 3 | |
| β-strand | 136-137 | 2 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 3 |
| α-helix | 12-20 | 9 | |
| β-strand | 26-30 | 5 | 3 |
| α-helix | 34-39 | 6 | |
| β-strand | 41-42 | 2 | 4 |
| β-strand | 46-47 | 2 | 3 |
| α-helix | 52-60 | 9 | |
| α-helix | 65-72 | 8 | |
| β-strand | 84-88 | 5 | 3 |
| α-helix | 103-112 | 10 | |
| β-strand | 118-122 | 5 | 3 |
| α-helix | 124-129 | 6 | |
| α-helix | 133-135 | 3 | |
| β-strand | 136-137 | 2 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-10 | 2 | 7 |
| α-helix | 12-20 | 9 | |
| β-strand | 26-30 | 5 | 7 |
| α-helix | 34-39 | 6 | |
| β-strand | 41-42 | 2 | 8 |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 52-60 | 9 | |
| α-helix | 65-70 | 6 | |
| β-strand | 84-88 | 5 | 7 |
| α-helix | 103-112 | 10 | |
| β-strand | 118-121 | 4 | 7 |
| α-helix | 124-131 | 8 | |
| α-helix | 133-135 | 3 | |
| β-strand | 136-137 | 2 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dual specificity protein phosphatase 16 | A, B, C, D | protein | 142 | Homo sapiens | Q9BY84 (AlphaFold model) |
>3TG3_1 Dual specificity protein phosphatase 16 (chains A, B, C, D) MIGTQIVTERLVALLESGTEKVLLIDSRPFVEYNTSHILEAININCSKLMKRRLQQDKVL ITELIQHSAKHKVDIDCSQKVVVYDQSSQDVASLSSDCFLTVLLGKLEKSFNSVHLLAGG FAEFSRCFPGLCEGLEHHHHHH
A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38alpha with the MAPK Binding Domain of the Phosphatase MKP5. Zhang, Y.Y., Wu, J.W., Wang, Z.X. Sci Signal (2011) 4:ra88-ra88. DOI 10.1126/scisignal.2002241 · PubMed
Other PDB entries of the same protein (UniProt Q9BY84 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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