3KUL

Kinase domain of human ephrin type-A receptor 8 (EPHA8)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Kinase Domain of Human Ephrin Type-A Receptor 8 (Epha8)

Walker, J.R.Yermekbayeva, L.Kania, J.Bountra, C.Weigelt, J.Arrowsmith, C.H.Edwards, A.M.Bochkarev, A.Dhe-Paganon, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ephrin type-A receptor 8325Homo sapiensMutation(s): 0 
Gene Names: EEKEPHA8HEK3KIAA1459
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for P29322 (Homo sapiens)
Explore P29322 
Go to UniProtKB:  P29322
PHAROS:  P29322
GTEx:  ENSG00000070886 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29322
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Ephrin type-A receptor 8325Homo sapiensMutation(s): 0 
Gene Names: EEKEPHA8HEK3KIAA1459
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for P29322 (Homo sapiens)
Explore P29322 
Go to UniProtKB:  P29322
PHAROS:  P29322
GTEx:  ENSG00000070886 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29322
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.14α = 90
b = 41.879β = 92.46
c = 145.815γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2009-12-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Non-polymer description, Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.3: 2023-11-22
    Changes: Data collection