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PDBsum entry 2xfo

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
2xfo
Jmol
Contents
Protein chain
499 a.a. *
Ligands
FA8-3PL
XCG ×2
FAD-3PL
Waters ×303
* Residue conservation analysis
PDB id:
2xfo
Name: Oxidoreductase
Title: Tranylcypromine-inhibited human monoamine oxidase b ile199ala mutant in complex with 2-(2-benzofuranyl)-2- imidazoline
Structure: Amine oxidase [flavin-containing] b. Chain: a, b. Synonym: monoamine oxidase type b, mao-b. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606
Resolution:
2.10Å     R-factor:   0.190     R-free:   0.243
Authors: D.Bonivento,E.M.Milczek,G.R.Mcdonald,C.Binda,A.Holt,D.E.Edmo A.Mattevi
Key ref: D.Bonivento et al. (2010). Potentiation of ligand binding through cooperative effects in monoamine oxidase B. J Biol Chem, 285, 36849-36856. PubMed id: 20855894 DOI: 10.1074/jbc.M110.169482
Date:
26-May-10     Release date:   06-Oct-10    
PROCHECK
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 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
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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 = FA8) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   7 terms 
  Biological process     small molecule metabolic process   16 terms 
  Biochemical function     electron carrier activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1074/jbc.M110.169482 J Biol Chem 285:36849-36856 (2010)
PubMed id: 20855894  
 
 
Potentiation of ligand binding through cooperative effects in monoamine oxidase B.
D.Bonivento, E.M.Milczek, G.R.McDonald, C.Binda, A.Holt, D.E.Edmondson, A.Mattevi.
 
  ABSTRACT  
 
No abstract given.