5X5W

Crystal structure of pseudorabies virus glycoprotein D


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.239 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal structure of pseudorabies virus glycoprotein D

Li, A.Lu, G.Qi, J.Wu, L.Tian, K.Luo, T.Shi, Y.Yan, J.Gao, G.F.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GD
A, C
402Suid alphaherpesvirus 1Mutation(s): 0 
Gene Names: US6
UniProt
Find proteins for G3G933 (Suid alphaherpesvirus 1)
Explore G3G933 
Go to UniProtKB:  G3G933
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupG3G933
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Nectin-1
B, D
107Sus scrofaMutation(s): 0 
Gene Names: NECTIN1HVECPRR1PVRL1
UniProt
Find proteins for Q9GL76 (Sus scrofa)
Explore Q9GL76 
Go to UniProtKB:  Q9GL76
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9GL76
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.266 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.239 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.945α = 90
b = 98.11β = 90
c = 128.395γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-04-26
    Type: Initial release
  • Version 1.1: 2023-11-22
    Changes: Data collection, Database references, Refinement description