4O38

Crystal structure of the human cyclin G associated kinase (GAK)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.165 
  • R-Value Observed: 0.166 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of the human cyclin G associated kinase (GAK)

Zhang, R.Hatzos-Skintges, C.Weger, A.Chaikuad, A.Eswaran, J.Fedorov, O.King, O.von Delft, F.Bountra, C.Arrowsmith, C.H.Weigelt, J.Edwards, A.Knapp, S.Joachimiak, A.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Cyclin-G-associated kinase
A, B
338Homo sapiensMutation(s): 0 
Gene Names: GAK
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for O14976 (Homo sapiens)
Explore O14976 
Go to UniProtKB:  O14976
PHAROS:  O14976
GTEx:  ENSG00000178950 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO14976
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.195 
  • R-Value Work: 0.165 
  • R-Value Observed: 0.166 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 103.425α = 90
b = 103.425β = 90
c = 131.951γ = 120
Software Package:
Software NamePurpose
SBC-Collectdata collection
HKL-3000phasing
REFMACrefinement
HKL-3000data reduction
HKL-3000data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2014-01-01
    Type: Initial release
  • Version 1.1: 2017-11-22
    Changes: Refinement description