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seesar software v.9.0  (BioSolveIT GmbH)

 
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    Structured Review

    BioSolveIT GmbH seesar software v.9.0
    Visualization of the crystal structures of <t>h</t> <t>MAO-A</t> and h MAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer h MAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with h MAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of h MAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in <t>SeeSAR:</t> green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).
    Seesar Software V.9.0, supplied by BioSolveIT GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/seesar+software+v%2E9%2E0/pmc06549493-113-18-23?v=BioSolveIT+GmbH
    Average 90 stars, based on 1 article reviews
    seesar software v.9.0 - by Bioz Stars, 2026-07
    90/100 stars

    Images

    1) Product Images from "Monoamine Oxidases (MAOs) as Privileged Molecular Targets in Neuroscience: Research Literature Analysis"

    Article Title: Monoamine Oxidases (MAOs) as Privileged Molecular Targets in Neuroscience: Research Literature Analysis

    Journal: Frontiers in Molecular Neuroscience

    doi: 10.3389/fnmol.2019.00143

    Visualization of the crystal structures of h MAO-A and h MAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer h MAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with h MAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of h MAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in SeeSAR: green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).
    Figure Legend Snippet: Visualization of the crystal structures of h MAO-A and h MAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer h MAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with h MAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of h MAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in SeeSAR: green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).

    Techniques Used: Binding Assay, Inhibition, Membrane



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    seesar software v.9.0  (BioSolveIT GmbH)
    90
    BioSolveIT GmbH seesar software v.9.0
    Visualization of the crystal structures of <t>h</t> <t>MAO-A</t> and h MAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer h MAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with h MAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of h MAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in <t>SeeSAR:</t> green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).
    Seesar Software V.9.0, supplied by BioSolveIT GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/seesar+software+v%2E9%2E0/pmc06549493-113-18-23?v=BioSolveIT+GmbH
    Average 90 stars, based on 1 article reviews
    seesar software v.9.0 - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Visualization of the crystal structures of h MAO-A and h MAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer h MAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with h MAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of h MAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in SeeSAR: green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Monoamine Oxidases (MAOs) as Privileged Molecular Targets in Neuroscience: Research Literature Analysis

    doi: 10.3389/fnmol.2019.00143

    Figure Lengend Snippet: Visualization of the crystal structures of h MAO-A and h MAO-B. The binding mode of irreversible and reversible MAO inhibition on the example of the most prominent MAO-A inhibitor clorgyline (irreversible) and MAO-B inhibitor safinamide (reversible) is represented. (A) Ribbon representation of the co-crystallized structure of clorgyline with the monomer h MAO-A (PDB: 2BXS, resolution: 3.15 Å). The C-terminal membrane region and the N-terminus are depicted. The surface for binding site is colored in gray transparent. (B) Representation of the covalent bonding (1.38 Å) between the irreversible MAO-A inhibitor clorgyline and the FAD co-factor. (C) Ribbon representation of the co-crystallized structure of safinamide with h MAO-B (PDB: 2V5Z, resolution: 1.6 Å). The respective chain A and B of h MAO-B dimer with FAD are depicted. (D) HYDE (HYdrogen bonding and DEsolvation) analysis of desolvation effects and interactions for safinamide (off-white). HYDE visual affinity assessment as embedded in SeeSAR: green = favorable, red = unfavorable and non-colored = no relevant for affinity. The interacting amino acid residues, important water molecules and FAD are shown. Visualization and HYDE analysis were performed using the SeeSAR tool from BioSolveIT (v.8.2, 2019).

    Article Snippet: Visualization of the 3D crystal structures of the human MAO-A and human MAO-B enzyme was performed with the SeeSAR software (v.9.0, 2019 form BioSolveIT).

    Techniques: Binding Assay, Inhibition, Membrane