6FEL

Structure of 14-3-3 gamma in complex with CaMKK2 14-3-3 binding motif Ser511

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.84 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.230 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history. 


Literature

14-3-3 protein directly interacts with the kinase domain of calcium/calmodulin-dependent protein kinase kinase (CaMKK2).

Psenakova, K., Petrvalska, O., Kylarova, S., Lentini Santo, D., Kalabova, D., Herman, P., Obsilova, V., Obsil, T.

(2018) Biochim Biophys Acta 1862: 1612-1625

  • DOI: https://doi.org/10.1016/j.bbagen.2018.04.006
  • Primary Citation of Related Structures:  
    6EWW, 6FEL

  • PubMed Abstract: 

    Calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2) is a member of the Ca 2+ /calmodulin-dependent kinase (CaMK) family involved in adiposity regulation, glucose homeostasis and cancer. This upstream activator of CaMKI, CaMKIV and AMP-activated protein kinase is inhibited by phosphorylation, which also triggers an association with the scaffolding protein 14-3-3. However, the role of 14-3-3 in the regulation of CaMKK2 remains unknown.

    • Organizational Affiliation: 

    Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, Prague, Czech Republic; BioCeV - Institute of Physiology, The Czech Academy of Sciences, Vestec, Czech Republic.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
14-3-3 protein gammaA,
B [auth C],
C [auth B],
D		236Homo sapiensMutation(s): 0 
Gene Names: YWHAG
UniProt & NIH Common Fund Data Resources
Find proteins for P61981 (Homo sapiens)
Explore P61981 
Go to UniProtKB:  P61981
PHAROS:  P61981
GTEx:  ENSG00000170027 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP61981
Sequence Annotations
Expand
  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Calcium/calmodulin-dependent protein kinase kinase 2
E, F, G, H
8Homo sapiensMutation(s): 0 
EC: 2.7.11.17
UniProt & NIH Common Fund Data Resources
Find proteins for Q96RR4 (Homo sapiens)
Explore Q96RR4 
Go to UniProtKB:  Q96RR4
PHAROS:  Q96RR4
GTEx:  ENSG00000110931 
Entity Groups  
UniProt GroupQ96RR4
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
SEP
Query on SEP
E, F, G, H
L-PEPTIDE LINKINGC3 H8 N O6 PSER
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.84 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.230 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 115.734α = 90
b = 115.734β = 90
c = 203.963γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
XDSdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Czech Science FoundationCzech Republic16-02739S

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-10
    Type: Initial release
  • Version 1.1: 2018-01-24
    Changes: Source and taxonomy
  • Version 1.2: 2018-04-25
    Changes: Data collection, Database references
  • Version 1.3: 2018-05-23
    Changes: Data collection, Database references
  • Version 1.4: 2019-11-06
    Changes: Data collection
  • Version 1.5: 2024-01-17
    Changes: Data collection, Database references, Refinement description