2WML

Crystal Structure of a Mammalian Sialyltransferase

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.213 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.175 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Structural Insight Into Mammalian Sialyltransferases.

Rao, F.V., Rich, J.R., Rakic, B., Buddai, S., Schwartz, M.F., Johnson, K., Bowe, C., Wakarchuk, W.W., Defrees, S., Withers, S.G., Strynadka, N.C.J.

(2009) Nat Struct Mol Biol 16: 1186

  • DOI: https://doi.org/10.1038/nsmb.1685
  • Primary Citation of Related Structures:  
    2WML

  • PubMed Abstract: 

    Mammalian cell surfaces are modified by complex arrays of glycoproteins, glycolipids and polysaccharides, many of which terminate in sialic acid and have central roles in essential processes including cell recognition, adhesion and immunogenicity. Sialylation of glycoconjugates is performed by a set of sequence-related enzymes known as sialyltransferases (STs). Here we present the crystal structure of a mammalian ST, porcine ST3Gal-I, providing a structural basis for understanding the mechanism and specificity of these enzymes and for the design of selective inhibitors.

    • Organizational Affiliation: 

    Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, Canada.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CMP-N-ACETYLNEURAMINATE-BETA-GALACTOSAMIDE -ALPHA-2\,3-SIALYLTRANSFERASE298Sus scrofaMutation(s): 0 
EC: 2.4.99.4
UniProt
Find proteins for Q02745 (Sus scrofa)
Explore Q02745 
Go to UniProtKB:  Q02745
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ02745
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: 1.90 Å
  • R-Value Free: 0.213 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.175 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 73.378α = 90
b = 78.01β = 90
c = 98.525γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
SOLVEphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-10-13
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2011-11-16
    Changes: Database references, Derived calculations, Non-polymer description, Other, Structure summary