Crystal structure of the Cbk1(T743E)-Mob2 kinase-coactivator complex, in crystal form A. Determined by X-ray diffraction at 4.5 Å resolution. Released 30 Jul 2014.
Explore 4LQP in 3D Show helices and sheets RCSB PDB PDBe
4LQP contains 21 α-helices and 10 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 |
|---|---|---|---|
| α-helix | 299-315 | 17 | |
| α-helix | 318-320 | 3 | |
| β-strand | 339 | 1 | 1 |
| β-strand | 352-360 | 9 | 2 |
| β-strand | 365-371 | 7 | 2 |
| β-strand | 378-384 | 7 | 2 |
| α-helix | 413-414 | 2 | |
| β-strand | 415-420 | 6 | 2 |
| β-strand | 424-430 | 7 | 2 |
| β-strand | 436 | 1 | 3 |
| α-helix | 437-443 | 7 | |
| α-helix | 452-468 | 17 | |
| α-helix | 478-480 | 3 | |
| β-strand | 482-483 | 2 | 3 |
| β-strand | 489-490 | 2 | 3 |
| α-helix | 590-605 | 16 | |
| α-helix | 621-625 | 5 | |
| α-helix | 627-629 | 3 | |
| α-helix | 640-649 | 10 | |
| α-helix | 679-681 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-117 | 2 | |
| β-strand | 120 | 1 | 1 |
| α-helix | 122-141 | 20 | |
| α-helix | 183-193 | 11 | |
| α-helix | 196-198 | 3 | |
| α-helix | 211-228 | 18 | |
| α-helix | 229-233 | 5 | |
| α-helix | 234-240 | 7 | |
| α-helix | 243-260 | 18 | |
| α-helix | 266-271 | 6 | |
| α-helix | 272-275 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase CBK1 | A | protein | 508 | Saccharomyces cerevisiae | P53894 (AlphaFold model) |
| CBK1 kinase activator protein MOB2 | B | protein | 244 | Saccharomyces cerevisiae | P43563 (AlphaFold model) |
>4LQP_1 Serine/threonine-protein kinase CBK1 (chains A) GSSPVQSGFNNGTISNYMYFERRPDLLTKGTQDKAAAVKLKIENFYQSSVKYAIERNERR VELETELTSHNWSEERKSRQLSSLGKKESQFLRLRRTRLSLEDFHTVKVIGKGAFGEVRL VQKKDTGKIYAMKTLLKSEMYKKDQLAHVKAERDVLAGSDSPWVVSLYYSFQDAQYLYLI MEFLPGGDLMTMLIRWQLFTEDVTRFYMAECILAIETIHKLGFIHRAIKPDNILIDIRGH IKLSDFGLSTGFHKTHDSNYYKKLLQQDEATNGISKPGTYNANTTDTANKRQTMVVDSIS LTMSNRQQIQTWRKSRRLMAYSTVGTPDYIAPEIFLYQGYGQECDWWSLGAIMYECLIGW PPFCSETPQETYRKIMNFEQTLQFPDDIHISYEAEDLIRRLLTHADQRLGRHGGADEIKS HPFFRGVDWNTIRQVEAPYIPKLSSITDTRFFPTDELENVPDSPAMAQAAKQREQMTKQG GSAPVKEDLPFIGYEYSRFDYLTRKNAL
>4LQP_2 CBK1 kinase activator protein MOB2 (chains B) GSRNKHHSPKRHSQTSFPAQKSTPQSQQLTSTTPQSQQQEASERSESQQIMFLSEPFVRT ALVKGSFKTIVQLPKYVDLGEWIALNVFEFFTNLNQFYGVVAEYVTPDAYPTMNAGPHTD YLWLDANNRQVSLPASQYIDLALTWINNKVNDKNLFPTKNGLPFPQQFSRDVQRIMVQMF RIFAHIYHHHFDKIVHLSLEAHWNSFFSHFISFAKEFKIIDRKEMAPLLPLIESFEKQGK IIYN
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
The Structure of an NDR/LATS Kinase-Mob Complex Reveals a Novel Kinase-Coactivator System and Substrate Docking Mechanism. Gogl, G., Schneider, K.D., Yeh, B.J. et al. PLoS Biol (2015) 13:e1002146-e1002146. DOI 10.1371/journal.pbio.1002146 · PubMed
Other PDB entries of the same protein (UniProt P53894 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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