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PDBsum entry 3po7

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protein ligands Protein-protein interface(s) links
Oxidoreductase/oxidoreductase inhibitor PDB id
3po7
Jmol
Contents
Protein chain
499 a.a. *
Ligands
FAD ×2
ZON ×2
Waters ×749
* Residue conservation analysis
PDB id:
3po7
Name: Oxidoreductase/oxidoreductase inhibitor
Title: Human monoamine oxidase b in complex with zonisamide
Structure: Amine oxidase [flavin-containing] b. Chain: a, b. Synonym: monoamine oxidase type b, mao-b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Resolution:
1.80Å     R-factor:   0.183     R-free:   0.212
Authors: C.Binda,M.Aldeco,A.Mattevi,D.E.Edmondson
Key ref: C.Binda et al. (2011). Interactions of monoamine oxidases with the antiepileptic drug zonisamide: specificity of inhibition and structure of the human monoamine oxidase B complex. J Med Chem, 54, 909-912. PubMed id: 21175212
Date:
22-Nov-10     Release date:   12-Jan-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P27338  (AOFB_HUMAN) -  Amine oxidase [flavin-containing] B
Seq:
Struc:
 
Seq:
Struc:
520 a.a.
499 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.4.3.4  - Monoamine oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2
RCH(2)NHR'
+ H(2)O
+ O(2)
= RCHO
+ R'NH(2)
+ H(2)O(2)
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   6 terms 
  Biological process     small molecule metabolic process   14 terms 
  Biochemical function     electron carrier activity     5 terms  

 

 
    reference    
 
 
J Med Chem 54:909-912 (2011)
PubMed id: 21175212  
 
 
Interactions of monoamine oxidases with the antiepileptic drug zonisamide: specificity of inhibition and structure of the human monoamine oxidase B complex.
C.Binda, M.Aldeco, A.Mattevi, D.E.Edmondson.
 
  ABSTRACT  
 
The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has been investigated. It is a competitive inhibitor of human MAO B (K(i) = 3.1 ± 0.3 μM), of rat MAO B (K(i) = 2.9 ± 0.5 μM), and of zebrafish MAO (K(i) = 30.8 ± 5.3 μM). No inhibition is observed with purified human or rat MAO A. The 1.8 Å structure of the MAO B complex demonstrates that it binds within the substrate cavity.