3L8M

Crystal Structure of a probable thiamine pyrophosphokinase from Staphylococcus saprophyticus subsp. saprophyticus. Northeast Structural Genomics Consortium target id SyR86

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.238 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history. 


Literature

Crystal Structure of a probable thiamine pyrophosphokinase from Staphylococcus saprophyticus subsp. saprophyticus. Northeast Structural Genomics Consortium target id SyR86

Seetharaman, J., Lew, S., Wang, D., Janjua, H., Cunningham, K., Owens, L., Xiao, R., Liu, J., Baran, M.C., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L., Northeast Structural Genomics Consortium (NESG)

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
probable thiamine pyrophosphokinase
A, B
212Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 = NCTC 7292Mutation(s): 0 
Gene Names: SSP1549
UniProt
Find proteins for Q49X04 (Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41))
Explore Q49X04 
Go to UniProtKB:  Q49X04
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ49X04
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.271 
  • R-Value Work: 0.238 
  • R-Value Observed: 0.238 
  • Space Group: P 63
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.873α = 90
b = 101.873β = 90
c = 88.024γ = 120
Software Package:
Software NamePurpose
ADSCdata collection
SHELXSphasing
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-02-09
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance