2V5Z

Structure of human MAO B in complex with the selective inhibitor safinamide

Summary for 2V5Z

• Entry DOI: 10.2210/pdb2v5z/pdb
• Related: 1GOS 1H8R 1OJ9 1OJA 1OJB 1OJC 1OJD 1S2Q 1S2Y 1S3B 1S3E 2BK3 2BK4 2BK5 2BYB 2C64 2C65 2C66 2C67 2C70 2C72 2C73 2C75 2C76
• Descriptor: Amine oxidase [flavin-containing] B, FLAVIN-ADENINE DINUCLEOTIDE, (S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE], ... (4 entities in total)
• Functional Keywords: fad, membrane, safinamide, flavoprotein, human mao b structure, reversible inhibitor binding, mitochondrion, transmembrane, oxidoreductase, neuroprotection, parkinson's disease
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side:
• Total number of polymer chains: 2
• Total formula weight: 119847.21

Authors

Binda, C.,Wang, J.,Pisani, L.,Caccia, C.,Carotti, A.,Salvati, P.,Edmondson, D.E.,Mattevi, A. (deposition date: 2007-07-12, release date: 2007-10-16, Last modification date: 2024-02-07)

Primary citation

Binda, C.,Wang, J.,Pisani, L.,Caccia, C.,Carotti, A.,Salvati, P.,Edmondson, D.E.,Mattevi, A.
Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs.
J.Med.Chem., 50:5848-5852, 2007

PubMed Abstract: Structures of human monoamine oxidase B (MAO B) in complex with safinamide and two coumarin derivatives, all sharing a common benzyloxy substituent, were determined by X-ray crystallography. These compounds competitively inhibit MAO B with Ki values in the 0.1-0.5 microM range that are 30-700-fold lower than those observed with MAO A. The inhibitors bind noncovalently to MAO B, occupying both the entrance and the substrate cavities and showing a similarly oriented benzyloxy substituent.

PubMed: 17915852
DOI: 10.1021/jm070677y

Experimental method

X-RAY DIFFRACTION (1.6 Å)