Crystal structure of human unphosphorylated p38gamma. Determined by X-ray diffraction at 3.15 Å resolution. Released 30 Jun 2021.
Explore 7CGA in 3D Show helices and sheets RCSB PDB PDBe
7CGA contains 63 α-helices and 57 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 | 11-16 | 6 | 1 |
| β-strand | 19-24 | 6 | 1 |
| β-strand | 27-35 | 9 | 2 |
| β-strand | 39-46 | 8 | 2 |
| β-strand | 52-58 | 7 | 2 |
| α-helix | 65-80 | 16 | |
| β-strand | 83 | 1 | 3 |
| β-strand | 86 | 1 | 3 |
| β-strand | 91-93 | 3 | 2 |
| α-helix | 99-101 | 3 | |
| β-strand | 106-110 | 5 | 2 |
| β-strand | 114-115 | 2 | 3 |
| α-helix | 118-121 | 4 | |
| α-helix | 129-146 | 18 | |
| β-strand | 149-150 | 2 | 4 |
| α-helix | 156-158 | 3 | |
| β-strand | 159-161 | 3 | 3 |
| β-strand | 167-169 | 3 | 3 |
| β-strand | 176-177 | 2 | 4 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-221 | 16 | |
| α-helix | 231-242 | 12 | |
| α-helix | 246-249 | 4 | |
| α-helix | 256-263 | 8 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-291 | 10 | |
| α-helix | 300-301 | 2 | |
| α-helix | 302-306 | 5 | |
| α-helix | 309-314 | 6 | |
| α-helix | 324-326 | 3 | |
| α-helix | 329-332 | 4 | |
| α-helix | 337-349 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-16 | 6 | 5 |
| β-strand | 19-24 | 6 | 5 |
| β-strand | 28-36 | 9 | 6 |
| β-strand | 39-45 | 7 | 6 |
| β-strand | 52-58 | 7 | 6 |
| α-helix | 65-79 | 15 | |
| β-strand | 83 | 1 | 7 |
| β-strand | 86 | 1 | 7 |
| β-strand | 91-93 | 3 | 6 |
| β-strand | 106-110 | 5 | 6 |
| β-strand | 115 | 1 | 7 |
| α-helix | 116-122 | 7 | |
| α-helix | 124-126 | 3 | |
| α-helix | 127-146 | 20 | |
| β-strand | 149-150 | 2 | 8 |
| α-helix | 156-158 | 3 | |
| β-strand | 159-161 | 3 | 7 |
| β-strand | 167-169 | 3 | 7 |
| β-strand | 176-177 | 2 | 8 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-221 | 16 | |
| α-helix | 231-242 | 12 | |
| α-helix | 256-264 | 9 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-291 | 10 | |
| α-helix | 302-306 | 5 | |
| α-helix | 309-311 | 3 | |
| α-helix | 324-326 | 3 | |
| α-helix | 337-350 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-15 | 5 | 9 |
| β-strand | 19 | 1 | 5 |
| β-strand | 20-24 | 5 | 9 |
| β-strand | 27-32 | 6 | 10 |
| β-strand | 39-46 | 8 | 10 |
| β-strand | 52-58 | 7 | 10 |
| α-helix | 65-80 | 16 | |
| β-strand | 83 | 1 | 11 |
| β-strand | 86 | 1 | 11 |
| β-strand | 91-93 | 3 | 10 |
| α-helix | 99-101 | 3 | |
| β-strand | 106-110 | 5 | 10 |
| β-strand | 114-115 | 2 | 11 |
| α-helix | 127-146 | 20 | |
| β-strand | 149-150 | 2 | 12 |
| α-helix | 156-158 | 3 | |
| β-strand | 159-161 | 3 | 11 |
| β-strand | 167-169 | 3 | 11 |
| β-strand | 176-177 | 2 | 12 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-221 | 16 | |
| α-helix | 231-242 | 12 | |
| α-helix | 247-251 | 5 | |
| α-helix | 256-263 | 8 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-291 | 10 | |
| α-helix | 302-307 | 6 | |
| α-helix | 309-311 | 3 | |
| α-helix | 324-326 | 3 | |
| α-helix | 337-349 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-16 | 6 | 13 |
| β-strand | 19-24 | 6 | 13 |
| β-strand | 27-36 | 10 | 14 |
| β-strand | 39-46 | 8 | 14 |
| β-strand | 52-58 | 7 | 14 |
| α-helix | 65-79 | 15 | |
| β-strand | 83 | 1 | 15 |
| β-strand | 86 | 1 | 15 |
| β-strand | 91-93 | 3 | 14 |
| β-strand | 106-110 | 5 | 14 |
| β-strand | 114-115 | 2 | 15 |
| α-helix | 116-122 | 7 | |
| α-helix | 127-146 | 20 | |
| β-strand | 149-150 | 2 | 16 |
| α-helix | 156-158 | 3 | |
| β-strand | 159-161 | 3 | 15 |
| β-strand | 167-169 | 3 | 15 |
| β-strand | 176-177 | 2 | 16 |
| α-helix | 194-198 | 5 | |
| α-helix | 207-221 | 15 | |
| α-helix | 231-242 | 12 | |
| α-helix | 256-263 | 8 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-291 | 10 | |
| α-helix | 300-301 | 2 | |
| α-helix | 302-306 | 5 | |
| α-helix | 309-311 | 3 | |
| α-helix | 324-326 | 3 | |
| α-helix | 337-349 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 12 | A, B, C, D | protein | 348 | Homo sapiens | P53778 (AlphaFold model) |
>7CGA_1 Mitogen-activated protein kinase 12 (chains A, B, C, D) SNASGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSE LFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKL GEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGY VVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTP PAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEA LAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKP
Structural basis for allosteric regulation of protein tyrosine phosphatase PTPN3 by unphosphorylated MAP kinase p38g. Hsu, S.F., Chen, K.E., Lee, C.C. et al. To be published.
Other PDB entries of the same protein (UniProt P53778 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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