4L4Q

Methionine Adenosyltransferase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structural and functional characterisation of the methionine adenosyltransferase from Thermococcus kodakarensis.

Schlesier, J.Siegrist, J.Gerhardt, S.Erb, A.Blaesi, S.Richter, M.Einsle, O.Andexer, J.N.

(2013) BMC Struct Biol 13: 22-22

  • DOI: https://doi.org/10.1186/1472-6807-13-22
  • Primary Citation of Related Structures:  
    4L4Q

  • PubMed Abstract: 

    Methionine adenosyltransferases catalyse the synthesis of S-adenosylmethionine, a cofactor abundant in all domains of life. In contrast to the enzymes from bacteria and eukarya that show high sequence similarity, methionine adenosyltransferases from archaea diverge on the amino acid sequence level and only few conserved residues are retained.


  • Organizational Affiliation

    Institute of Pharmaceutical Sciences, Albert-Ludwigs-University Freiburg, Albertstr, 25, Freiburg D-79104, Germany. jennifer.andexer@pharmazie.uni-freiburg.de.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
S-adenosylmethionine synthase
A, B, C, D
405Thermococcus kodakarensisMutation(s): 0 
Gene Names: matmetKTK0545
EC: 2.5.1.6
UniProt
Find proteins for Q5JF22 (Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1))
Explore Q5JF22 
Go to UniProtKB:  Q5JF22
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5JF22
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.245 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.190 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 134.839α = 90
b = 57.792β = 103.95
c = 236.434γ = 90
Software Package:
Software NamePurpose
ALBULAdata collection
SHARPphasing
REFMACrefinement
XDSdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-03-19
    Type: Initial release
  • Version 1.1: 2024-02-28
    Changes: Data collection, Database references