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PDBsum entry 2xfq

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
2xfq

 

 

 

 

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Contents
Protein chain
499 a.a. *
Ligands
FAD-RAS ×2
XCG ×2
C15
Waters ×472
* Residue conservation analysis
PDB id:
2xfq
Name: Oxidoreductase
Title: Rasagiline-inhibited human monoamine oxidase b in complex with 2-(2- benzofuranyl)-2-imidazoline
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: komagataella pastoris. Expression_system_taxid: 4922
Resolution:
2.20Å     R-factor:   0.159    
Authors: D.Bonivento,E.M.Milczek,G.R.Mcdonald,C.Binda,A.Holt,D.E.Edmondson, 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
Date:
26-May-10     Release date:   06-Oct-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 Enzyme reactions 
   Enzyme class 2: E.C.1.4.3.21  - primary-amine oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a primary methyl amine + O2 + H2O = an aldehyde + H2O2 + NH4+
primary methyl amine
+ O2
+ H2O
= aldehyde
+ H2O2
+ NH4(+)
   Enzyme class 3: E.C.1.4.3.4  - monoamine oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a secondary aliphatic amine + O2 + H2O = a primary amine + an aldehyde + H2O2
secondary aliphatic amine
+ O2
+ H2O
= primary amine
+ aldehyde
+ H2O2
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
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.

 

 

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