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PDBsum entry 4dok

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protein ligands metals Protein-protein interface(s) links
Isomerase PDB id
4dok
Jmol
Contents
Protein chains
208 a.a.
Ligands
ACT
Metals
_CA ×3
Waters ×356
PDB id:
4dok
Name: Isomerase
Title: Crystal structure of arabidopsis thaliana chalcone-isomerase protein at5g05270 (atchil)
Structure: Similarity to chalcone-flavonone isomerase. Chain: a, b. Engineered: yes
Source: Arabidopsis thaliana. Mouse-ear cress,thale-cress. Organism_taxid: 3702. Gene: at5g05270. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.70Å     R-factor:   0.192     R-free:   0.219
Authors: J.P.Noel,G.V.Louie,M.E.Bowman
Key ref: M.N.Ngaki et al. (2012). Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis. Nature, 485, 530-533. PubMed id: 22622584
Date:
09-Feb-12     Release date:   09-May-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8VZW3  (Q8VZW3_ARATH) -  Probable chalcone--flavonone isomerase 3
Seq:
Struc:
209 a.a.
208 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.5.5.1.6  - Chalcone isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Flavonoid Biosynthesis
      Reaction: A chalcone = a flavanone
chalcone
= flavanone
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     response to karrikin   5 terms 
  Biochemical function     isomerase activity     3 terms  

 

 
    Added reference    
 
 
Nature 485:530-533 (2012)
PubMed id: 22622584  
 
 
Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis.
M.N.Ngaki, G.V.Louie, R.N.Philippe, G.Manning, F.Pojer, M.E.Bowman, L.Li, E.Larsen, E.S.Wurtele, J.P.Noel.
 
  ABSTRACT  
 
No abstract given.