2AJ2

X-Ray Crystal Structure of Protein VC0467 from Vibrio cholerae. Northeast Structural Genomics Consortium Target VcR8.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.21 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.258 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

X-Ray structure of hypothetical protein VC0467 from Vibrio cholerae: new fold. Northeast Structural Genomics Consortium target VcR8.

Kuzin, A.P.Abashidze, M.Vorobiev, S.M.Acton, T.Xiao, R.Conover, K.Ma, L.-C.Kellie, R.Montelione, G.T.Hunt, J.F.Tong, L.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Hypothetical UPF0301 protein VC0467208Vibrio choleraeMutation(s): 8 
UniProt
Find proteins for Q9KUP8 (Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961))
Explore Q9KUP8 
Go to UniProtKB:  Q9KUP8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9KUP8
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.21 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.258 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 58.351α = 90
b = 58.351β = 90
c = 251.976γ = 120
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2005-09-20
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance