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PDBsum entry 3oe4

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protein ligands metals links
Transferase/transferase inhibitor PDB id
3oe4
Jmol
Contents
Protein chain
213 a.a.
Ligands
610
Metals
_MG
Waters ×161
PDB id:
3oe4
Name: Transferase/transferase inhibitor
Title: Rat catechol o-methyltransferase in complex with a catechol- purine-containing bisubstrate inhibitor - humanized form
Structure: Catechol o-methyltransferase. Chain: a. Fragment: soluble form, unp residues 44-264. Engineered: yes. Mutation: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Tissue: liver. Gene: comt. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.49Å     R-factor:   0.180     R-free:   0.203
Authors: A.Ehler,D.Schlatter,M.Stihle,J.Benz,M.G.Rudolph
Key ref: M.Ellermann et al. (2011). Molecular recognition at the active site of catechol-O-methyltransferase (COMT): adenine replacements in bisubstrate inhibitors. Chemistry, 17, 6369-6381. PubMed id: 21538606
Date:
12-Aug-10     Release date:   16-Mar-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P22734  (COMT_RAT) -  Catechol O-methyltransferase
Seq:
Struc:
264 a.a.
213 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.2.1.1.6  - Catechol O-methyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
S-adenosyl-L-methionine
+ catechol
=
S-adenosyl-L-homocysteine
Bound ligand (Het Group name = 610)
matches with 40.48% similarity
+ guaiacol
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     neurotransmitter catabolic process   2 terms 
  Biochemical function     magnesium ion binding     3 terms  

 

 
    reference    
 
 
Chemistry 17:6369-6381 (2011)
PubMed id: 21538606  
 
 
Molecular recognition at the active site of catechol-O-methyltransferase (COMT): adenine replacements in bisubstrate inhibitors.
M.Ellermann, R.Paulini, R.Jakob-Roetne, C.Lerner, E.Borroni, D.Roth, A.Ehler, W.B.Schweizer, D.Schlatter, M.G.Rudolph, F.Diederich.
 
  ABSTRACT  
 
No abstract given.