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PDBsum entry 2h0v

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2h0v
Jmol
Contents
Protein chains
335 a.a. *
Ligands
EDO ×18
TLA ×2
TRS ×2
Metals
_FE ×4
Waters ×312
* Residue conservation analysis
PDB id:
2h0v
Name: Oxidoreductase
Title: Crystal structure of a putative quercetin 2,3-dioxygenase (y bsu39980) from bacillus subtilis at 2.60 a resolution
Structure: Quercetin 2,3-dioxygenase. Chain: a, b. Synonym: quercetinase, flavonol 2,4-dioxygenase. Engineered: yes
Source: Bacillus subtilis. Organism_taxid: 1423. Gene: qdoi. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.60Å     R-factor:   0.169     R-free:   0.204
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref: Joint center for structural genomics (jcsg) Crystal structure of (2636545) from bacillus subtilis 2.60 a resolution. To be published, .
Date:
15-May-06     Release date:   30-May-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P42106  (QDOI_BACSU) -  Quercetin 2,3-dioxygenase
Seq:
Struc:
337 a.a.
335 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.13.11.24  - Quercetin 2,3-dioxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Quercetin 2,3-Dioxygenase
      Reaction: Quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
Quercetin
+ O(2)
= 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate
+
CO
Bound ligand (Het Group name = EDO)
matches with 50.00% similarity
+ H(+)
      Cofactor: Fe cation or Cu cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity     4 terms