Crystal structure of the Cbk1-Mob2 kinase-coactivator complex with an SSD1 peptide. Determined by X-ray diffraction at 3.15 Å resolution. Released 16 May 2018.
Explore 5NCL in 3D Show helices and sheets RCSB PDB PDBe
5NCL contains 26 α-helices and 9 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 | 281-315 | 35 | |
| α-helix | 322-344 | 23 | |
| β-strand | 353-360 | 8 | 1 |
| β-strand | 365-370 | 6 | 1 |
| β-strand | 378-384 | 7 | 1 |
| β-strand | 412 | 1 | 2 |
| α-helix | 413-414 | 2 | |
| β-strand | 415-420 | 6 | 1 |
| β-strand | 424-430 | 7 | 1 |
| β-strand | 436 | 1 | 2 |
| α-helix | 437-444 | 8 | |
| α-helix | 449-468 | 20 | |
| β-strand | 481-483 | 3 | 2 |
| β-strand | 489-491 | 3 | 2 |
| α-helix | 554-565 | 12 | |
| α-helix | 580-583 | 4 | |
| α-helix | 592-606 | 15 | |
| α-helix | 616-624 | 9 | |
| α-helix | 626-629 | 4 | |
| α-helix | 642-649 | 8 | |
| α-helix | 653-655 | 3 | |
| α-helix | 679-682 | 4 | |
| α-helix | 697-699 | 3 | |
| α-helix | 746-753 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 116-117 | 2 | |
| α-helix | 122-140 | 19 | |
| α-helix | 141-143 | 3 | |
| α-helix | 145-147 | 3 | |
| α-helix | 178-194 | 17 | |
| α-helix | 205-208 | 4 | |
| α-helix | 210-231 | 22 | |
| α-helix | 235-240 | 6 | |
| α-helix | 243-259 | 17 | |
| α-helix | 265-268 | 4 | |
| α-helix | 272-277 | 6 |
| 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) |
| Protein SSD1 | D | protein | 10 | Saccharomyces cerevisiae | P24276 (AlphaFold model) |
>5NCL_1 Serine/threonine-protein kinase CBK1 (chains A) GSSPVQSGFNNGTISNYMYFERRPDLLTKGTQDKAAAVKLKIENFYQSSVKYAIERNERR VELETELTSHNWSEERKSRQLSSLGKKESQFLRLRRTRLSLEDFHTVKVIGKGAFGEVRL VQKKDTGKIYAMKTLLKSEMYKKDQLAHVKAERDVLAGSDSPWVVSLYYSFQDAQYLYLI MEFLPGGDLMTMLIRWQLFTEDVTRFYMAECILAIETIHKLGFIHRAIKPDNILIDIRGH IKLSDFGLSTGFHKTHDSNYYKKLLQQDEATNGISKPGTYNANTTDTANKRQTMVVDSIS LTMSNRQQIQTWRKSRRLMAYSTVGTPDYIAPEIFLYQGYGQECDWWSLGAIMYECLIGW PPFCSETPQETYRKIMNFEQTLQFPDDIHISYEAEDLIRRLLTHADQRLGRHGGADEIKS HPFFRGVDWNTIRQVEAPYIPKLSSITDTRFFPTDELENVPDSPAMAQAAKQREQMTKQG GSAPVKEDLPFIGYTYSRFDYLTRKNAL
>5NCL_2 CBK1 kinase activator protein MOB2 (chains B) GSRNKHHSPKRHSQTSFPAQKSTPQSQQLTSTTPQSQQQEASERSESQQIMFLSEPFVRT ALVKGSFKTIVQLPKYVDLGEWIALNVFEFFTNLNQFYGVVAEYVTPDAYPTMNAGPHTD YLWLDANNRQVSLPASQYIDLALTWINNKVNDKNLFPTKNGLPFPQQFSRDVQRIMVQMF RIFAHIYHHHFDKIVHLSLEAHWNSFFSHFISFAKEFKIIDRKEMAPLLPLIESFEKQGK IIYN
>5NCL_3 Protein SSD1 (chains D) TTEQSDFKFP
| ID | Name | Formula | Copies |
|---|---|---|---|
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
Ndr/Lats Kinases Bind Specific Mob-Family Coactivators through a Conserved and Modular Interface. Parker, B.W., Gogl, G., Balint, M. et al. Biochemistry (2020). DOI 10.1021/acs.biochem.9b01096 · 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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