3PO7
Human monoamine oxidase B in complex with zonisamide
Summary for 3PO7
| Entry DOI | 10.2210/pdb3po7/pdb |
| Descriptor | Amine oxidase [flavin-containing] B, FLAVIN-ADENINE DINUCLEOTIDE, 1-(1,2-benzoxazol-3-yl)methanesulfonamide, ... (4 entities in total) |
| Functional Keywords | flavin-binding amine oxidase, neurotransmitter metabolism, fad, mitochondrial outer membrane, antiparkinson drug, oxidoreductase, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side: P27338 |
| Total number of polymer chains | 2 |
| Total formula weight | 119671.01 |
| Authors | Binda, C.,Aldeco, M.,Mattevi, A.,Edmondson, D.E. (deposition date: 2010-11-22, release date: 2011-01-12, Last modification date: 2024-11-06) |
| Primary citation | Binda, C.,Aldeco, M.,Mattevi, A.,Edmondson, D.E. 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, 2011 Cited by PubMed 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. PubMed: 21175212DOI: 10.1021/jm101359c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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