› 2v60

X-ray diffraction
2Å resolution

Structure of human MAO B in complex with the selective inhibitor 7-(3- chlorobenzyloxy)-4-carboxaldehyde-coumarin

Released:
DOI: 10.2210/pdb2v60/pdb
PDB entry 2v60 coloured by chain, front view.
PDB entry 2v60 coloured by chain, side view.
PDB entry 2v60 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human monoamine oxidase B complexes with selective noncovalent inhibitors: safinamide and coumarin analogs.
Binda C, Wang J, Pisani L, Caccia C, Carotti A, Salvati P, Edmondson DE, Mattevi A
J Med Chem 50 5848-52 (2007)
PMID: 17915852

Function and Biology Details

Reactions catalysed: 
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2)
RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150973 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amine oxidase [flavin-containing] B Chains: A, B
Molecule details ›
Chains: A, B
Length: 520 amino acids
Theoretical weight: 58.84 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P27338 (Residues: 1-520; Coverage: 100%)
Gene name: MAOB
Sequence domains: Flavin containing amine oxidoreductase
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand C17 2 x C17
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C222
Unit cell:
a: 130.694Å b: 224.413Å c: 86.811Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.221
Expression system: Komagataella pastoris

Quick links

Citations

40 review citations

Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases.
Edmondson et al. (2009)
39 more

19 mentions without citation

Molecular docking studies of coumarin hybrids as potential acetylcholinesterase, butyrylcholinesterase, monoamine oxidase A/B and β-amyloid inhibitors for Alzheimer's disease.
Yusufzai et al. (2018)
18 more