p38(alpha) MAP kinase with the activation loop of ERK2. Determined by X-ray diffraction at 1.66 Å resolution. Released 1 Apr 2020.
Explore 6QYX in 3D Show helices and sheets RCSB PDB PDBe
6QYX contains 24 α-helices and 11 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 5-7 | 3 | |
| β-strand | 8-12 | 5 | 1 |
| β-strand | 17-21 | 5 | 1 |
| β-strand | 24-33 | 10 | 2 |
| β-strand | 36-43 | 8 | 2 |
| β-strand | 48-54 | 7 | 2 |
| α-helix | 55 | 1 | |
| α-helix | 62-77 | 16 | |
| β-strand | 83 | 1 | 3 |
| β-strand | 88-90 | 3 | 2 |
| β-strand | 103-107 | 5 | 2 |
| β-strand | 111-112 | 2 | 3 |
| α-helix | 113-117 | 5 | |
| α-helix | 124-143 | 20 | |
| α-helix | 153-155 | 3 | |
| β-strand | 156-158 | 3 | 3 |
| β-strand | 164-166 | 3 | 3 |
| α-helix | 191-194 | 4 | |
| α-helix | 197-200 | 4 | |
| α-helix | 210-224 | 15 | |
| α-helix | 234-245 | 12 | |
| α-helix | 248-249 | 2 | |
| α-helix | 250-253 | 4 | |
| α-helix | 259-267 | 9 | |
| α-helix | 269-270 | 2 | |
| α-helix | 272-275 | 4 | |
| α-helix | 276-278 | 3 | |
| α-helix | 285-294 | 10 | |
| α-helix | 299-301 | 3 | |
| α-helix | 303-304 | 2 | |
| α-helix | 305-309 | 5 | |
| α-helix | 312-314 | 3 | |
| α-helix | 326-328 | 3 | |
| α-helix | 332-335 | 4 | |
| α-helix | 340-352 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase 14,Mitogen-activated protein kinase 1,Mitogen-activated protein… | A | protein | 366 | Homo sapiens, Crassostrea ariakensis | D2CIU1 (AlphaFold model), Q16539 (AlphaFold model) |
>6QYX_1 Mitogen-activated protein kinase 14,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 14 (chains A) MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQ SIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQ KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKICDFGLARVADPDHD HTGFLTEYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKL ILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSD KRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLD QEEMES
| ID | Name | Formula | Copies |
|---|---|---|---|
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 1 |
Water and common crystallization additives (EPE) are not listed.
The bacterial metalloprotease NleD selectively cleaves mitogen-activated protein kinases that have high flexibility in their activation loop. Gur-Arie, L., Eitan-Wexler, M., Weinberger, N. et al. J Biol Chem (2020) 295:9409-9420. DOI 10.1074/jbc.RA120.013590 · PubMed
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