PDBsum entry 3po7

Oxidoreductase/oxidoreductase inhibitor

PDB id: 3po7

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

Protein chains

P27338  (AOFB_HUMAN) -  Amine oxidase [flavin-containing] B from Homo sapiens

Seq: 520 a.a.

Struc: 499 a.a.

Enzyme reactions

• Enzyme class 2: E.C.1.4.3.21 - primary-amine oxidase.
• Reaction: a primary methyl amine + O2 + H2O = an aldehyde + H2O2 + NH4⁺
• Enzyme class 3: E.C.1.4.3.4 - monoamine oxidase.
• Reaction: a secondary aliphatic amine + O2 + H2O = a primary amine + an 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 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.