Crystal structure of inactive p38gamma. Determined by X-ray diffraction at 2.55 Å resolution. Released 18 Dec 2019.
Explore 6UNA in 3D Show helices and sheets RCSB PDB PDBe
6UNA contains 45 α-helices and 22 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 | 11-15 | 5 | 1 |
| β-strand | 18-24 | 7 | 2 |
| β-strand | 27-34 | 8 | 3 |
| β-strand | 39-46 | 8 | 3 |
| β-strand | 52-58 | 7 | 3 |
| α-helix | 65-80 | 16 | |
| β-strand | 86 | 1 | 4 |
| β-strand | 91-93 | 3 | 3 |
| α-helix | 99-101 | 3 | |
| β-strand | 106-110 | 5 | 3 |
| β-strand | 114-115 | 2 | 4 |
| α-helix | 116-122 | 7 | |
| α-helix | 127-146 | 20 | |
| α-helix | 156-158 | 3 | |
| β-strand | 159-161 | 3 | 4 |
| β-strand | 167-169 | 3 | 4 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-221 | 16 | |
| α-helix | 231-242 | 12 | |
| α-helix | 244-246 | 3 | |
| α-helix | 247-251 | 5 | |
| α-helix | 256-263 | 8 | |
| α-helix | 266-267 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-291 | 10 | |
| α-helix | 296-298 | 3 | |
| α-helix | 300-301 | 2 | |
| α-helix | 302-306 | 5 | |
| α-helix | 309-311 | 3 | |
| α-helix | 315-316 | 2 | |
| α-helix | 324-326 | 3 | |
| α-helix | 329-332 | 4 | |
| α-helix | 337-349 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-17 | 7 | 2 |
| β-strand | 20-24 | 5 | 1 |
| β-strand | 27-34 | 8 | 5 |
| β-strand | 39-46 | 8 | 5 |
| β-strand | 52-58 | 7 | 5 |
| α-helix | 65-80 | 16 | |
| β-strand | 86 | 1 | 6 |
| β-strand | 91-93 | 3 | 5 |
| α-helix | 99-101 | 3 | |
| β-strand | 106-110 | 5 | 5 |
| β-strand | 114-115 | 2 | 6 |
| α-helix | 116-122 | 7 | |
| α-helix | 127-146 | 20 | |
| α-helix | 156-158 | 3 | |
| β-strand | 159-161 | 3 | 6 |
| β-strand | 167-169 | 3 | 6 |
| α-helix | 194-197 | 4 | |
| α-helix | 206-221 | 16 | |
| α-helix | 231-242 | 12 | |
| α-helix | 244-246 | 3 | |
| α-helix | 247-251 | 5 | |
| α-helix | 256-263 | 8 | |
| α-helix | 266-267 | 2 | |
| α-helix | 269-272 | 4 | |
| α-helix | 273-276 | 4 | |
| α-helix | 282-291 | 10 | |
| α-helix | 296-298 | 3 | |
| α-helix | 302-306 | 5 | |
| α-helix | 309-311 | 3 | |
| α-helix | 315-316 | 2 | |
| α-helix | 320-321 | 2 | |
| α-helix | 324-326 | 3 | |
| α-helix | 337-349 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 12 | A, B | protein | 361 | Homo sapiens | P53778 (AlphaFold model) |
>6UNA_1 Mitogen-activated protein kinase 12 (chains A, B) ARSGFYRQEVTKTAWEVRAVYRDLRPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSEL FAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLG EDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYV VTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPP AEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEAL AHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKPPRQLGARVSKETP L
A Dynamic Switch in Inactive p38 gamma Leads to an Excited State on the Pathway to an Active Kinase. Aoto, P.C., Stanfield, R.L., Wilson, I.A. et al. Biochemistry (2019) 58:5160-5172. DOI 10.1021/acs.biochem.9b00932 · PubMed
Other PDB entries of the same protein (UniProt P53778 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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