4LQQ: Serine/threonine-protein kinase CBK1

Crystal structure of the Cbk1(T743E)-Mob2 kinase-coactivator complex in crystal form B. Determined by X-ray diffraction at 3.6 Å resolution. Released 30 Jul 2014.

Method
X-ray diffraction
Resolution
3.6 Å
Organism
Saccharomyces cerevisiae
Chains
4
Atoms
7,498
Mol. weight
174.91 kDa
Ligands
ANP
Released
30 Jul 2014

Explore 4LQQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LQQ contains 45 α-helices and 15 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.

Chain A: 14 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix295-2984
α-helix299-31618
α-helix317-3204
β-strand352-36091
β-strand365-37171
β-strand378-38471
β-strand415-42061
β-strand424-42961
β-strand43612
α-helix437-4437
α-helix450-4556
α-helix458-46811
α-helix478-4803
β-strand482-48322
β-strand489-49022
α-helix557-5604
α-helix561-5633
α-helix590-60617
α-helix621-6244
α-helix627-6293
α-helix640-65011
α-helix679-6813
Chain B: 10 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix112-1143
α-helix116-1172
α-helix122-14423
α-helix183-19311
α-helix211-22010
α-helix223-2286
α-helix229-2335
α-helix234-2407
α-helix243-25917
α-helix272-2754
Chain D: 13 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix297-2993
α-helix301-31616
β-strand352-35763
β-strand367-37153
β-strand378-38253
α-helix413-4142
β-strand415-41953
β-strand426-42943
α-helix437-4437
α-helix450-4556
α-helix458-46811
β-strand482-48324
β-strand489-49024
α-helix591-60616
α-helix616-6183
α-helix622-6254
α-helix627-6293
α-helix640-64910
α-helix666-6683
α-helix679-6813
Chain E: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix116-1172
α-helix122-14322
α-helix187-1937
α-helix211-22818
α-helix229-2335
α-helix234-2396
α-helix243-25917
α-helix272-2754

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein kinase CBK1A, Dprotein508Saccharomyces cerevisiaeP53894 (AlphaFold model)
CBK1 kinase activator protein MOB2B, Eprotein244Saccharomyces cerevisiaeP43563 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>4LQQ_1 Serine/threonine-protein kinase CBK1 (chains A, D)
GSSPVQSGFNNGTISNYMYFERRPDLLTKGTQDKAAAVKLKIENFYQSSVKYAIERNERR
VELETELTSHNWSEERKSRQLSSLGKKESQFLRLRRTRLSLEDFHTVKVIGKGAFGEVRL
VQKKDTGKIYAMKTLLKSEMYKKDQLAHVKAERDVLAGSDSPWVVSLYYSFQDAQYLYLI
MEFLPGGDLMTMLIRWQLFTEDVTRFYMAECILAIETIHKLGFIHRAIKPDNILIDIRGH
IKLSDFGLSTGFHKTHDSNYYKKLLQQDEATNGISKPGTYNANTTDTANKRQTMVVDSIS
LTMSNRQQIQTWRKSRRLMAYSTVGTPDYIAPEIFLYQGYGQECDWWSLGAIMYECLIGW
PPFCSETPQETYRKIMNFEQTLQFPDDIHISYEAEDLIRRLLTHADQRLGRHGGADEIKS
HPFFRGVDWNTIRQVEAPYIPKLSSITDTRFFPTDELENVPDSPAMAQAAKQREQMTKQG
GSAPVKEDLPFIGYEYSRFDYLTRKNAL
Sequence of entity 2 (B, E), FASTA
>4LQQ_2 CBK1 kinase activator protein MOB2 (chains B, E)
GSRNKHHSPKRHSQTSFPAQKSTPQSQQLTSTTPQSQQQEASERSESQQIMFLSEPFVRT
ALVKGSFKTIVQLPKYVDLGEWIALNVFEFFTNLNQFYGVVAEYVTPDAYPTMNAGPHTD
YLWLDANNRQVSLPASQYIDLALTWINNKVNDKNLFPTKNGLPFPQQFSRDVQRIMVQMF
RIFAHIYHHHFDKIVHLSLEAHWNSFFSHFISFAKEFKIIDRKEMAPLLPLIESFEKQGK
IIYN

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 4LQQ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.