3KF9

Crystal structure of the SdCen/skMLCK complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.204 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural features of the complexes formed by Scherffelia dubia centrin

Radu, L.Miron, S.Durand, D.Assairi, L.Blouquit, Y.Charbonnier, J.B.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Caltractin
A, C
149Scherffelia dubiaMutation(s): 0 
UniProt
Find proteins for Q06827 (Scherffelia dubia)
Explore Q06827 
Go to UniProtKB:  Q06827
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ06827
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Myosin light chain kinase 2, skeletal/cardiac muscle
B, D
22N/AMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for Q9H1R3 (Homo sapiens)
Explore Q9H1R3 
Go to UniProtKB:  Q9H1R3
PHAROS:  Q9H1R3
GTEx:  ENSG00000101306 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9H1R3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.204 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 40.75α = 90
b = 67.75β = 90
c = 129.53γ = 90
Software Package:
Software NamePurpose
MOLREPphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-01-26
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description