PDBsum entry 1dxi

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Isomerase(intramolecular oxidoreductase) PDB id
Protein chains
388 a.a. *
_MG ×4
Waters ×4
* Residue conservation analysis
PDB id:
Name: Isomerase(intramolecular oxidoreductase)
Title: Structure determination of glucose isomerase from streptomyc at 2.6 angstroms resolution
Structure: D-xylose isomerase. Chain: a, b. Engineered: yes
Source: Streptomyces murinus. Organism_taxid: 33900
Biol. unit: Tetramer (from PQS)
2.60Å     R-factor:   0.214    
Authors: H.Rasmussen,T.La Cour,J.Nyborg,M.Schulein
Key ref:
H.Rasmussen et al. (1994). Structure determination of glucose isomerase from Streptomyces murinus at 2.6 A resolution. Acta Crystallogr D Biol Crystallogr, 50, 124-131. PubMed id: 15299450 DOI: 10.1107/S0907444993009540
30-Sep-93     Release date:   31-Jan-94    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P37031  (XYLA_STRMR) -  Xylose isomerase
388 a.a.
388 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Xylose isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-xylopyranose = D-xylulose
= D-xylulose
      Cofactor: Magnesium
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     carbohydrate metabolic process   3 terms 
  Biochemical function     isomerase activity     4 terms  


    Key reference    
DOI no: 10.1107/S0907444993009540 Acta Crystallogr D Biol Crystallogr 50:124-131 (1994)
PubMed id: 15299450  
Structure determination of glucose isomerase from Streptomyces murinus at 2.6 A resolution.
H.Rasmussen, Cour, J.Nyborg, M.Schülein.
Glucose isomerase from Streptomyces murinus has been crystallized in space group P4(1)2(1)2, cell dimensions a = b = 137.65 and c = 132.20 A. One dimer of the tetrametric molecule is found per asymmetric unit. An initial structure solution was obtained by the molecular replacement method. The crystallographic refinement was performed using molecular dynamics techniques with X-ray restraints. The final crystallographic R value is 21.4% at 2.6 A resolution including 3023 non-H atoms, two metal ions and two water molecules per monomer.
  Selected figure(s)  
Figure 2.
Fig. 2. The average tmperature facor for the main­chain atoms of each residue for molecule A (solid line) and molecule B (dashed line) in the asymmetric unit.
Figure 3.
Fig. 3. Stereo drawing of the C of molecule A including the two Mg ons.
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1994, 50, 124-131) copyright 1994.  
  Figures were selected by an automated process.