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Oxidoreductase PDB id
1yw0
Jmol
Contents
Protein chains
243 a.a. *
Metals
_MG ×8
Waters ×105
* Residue conservation analysis
PDB id:
1yw0
Name: Oxidoreductase
Title: Crystal structure of the tryptophan 2,3-dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.
Structure: Tryptophan 2,3-dioxygenase. Chain: a, b, c, d. Engineered: yes
Source: Xanthomonas campestris pv. Campestris str. Atcc 33913. Organism_taxid: 190485. Strain: pv. Campestris str. Atcc 33913. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
Resolution:
2.70Å     R-factor:   0.250     R-free:   0.294
Authors: S.M.Vorobiev,M.Abashidze,F.Forouhar,A.Kuzin,R.Xiao,M.Ciano, T.B.Aton,G.T.Montelione,J.F.Hunt,L.Tong,Northeast Structural Genomics Consortium (Nesg)
Key ref: S.M.Vorobiev et al. Crystal structure of the tryptophan 2,3-Dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.. To be published,
Date:
16-Feb-05     Release date:   15-Mar-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8PDA8  (T23O_XANCP) -  Tryptophan 2,3-dioxygenase
Seq:
Struc: 		298 a.a.
243 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.13.11.11  - Tryptophan 2,3-dioxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Tryptophan Catabolism
      Reaction: L-tryptophan + O2 = N-formyl-L-kynurenine
L-tryptophan
 + O(2)
 = N-formyl-L-kynurenine
      Cofactor: Heme
Heme
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation reduction   4 terms 
  Biochemical function     oxidoreductase activity     6 terms