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5 br trp chem impex  (Chem Impex International)


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    Structured Review

    Chem Impex International 5 br trp chem impex
    Electron density of bound substrates. Initial mF o − DF c density before placing the ligand is shown as a green mesh at 3σ and the final 2 mF o − DF c density is shown as a blue mesh at 1.5σ. ( a , b ) Bound Trp from PDB entry 8cje chain C . ( c , d ) Bound <t>5-Br-Trp</t> from PDB entry 8cjf chain A . The anomalous signal of bromine in 5-Br-Trp is shown as a yellow mesh (5σ).
    5 Br Trp Chem Impex, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/5+br+trp+chem+impex/pmc10306068-114-20-21
    Average 86 stars, based on 1 article reviews
    5 br trp chem impex - by Bioz Stars, 2026-10
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    Images

    1) Product Images from "Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF"

    Article Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF

    Journal: Acta Crystallographica. Section D, Structural Biology

    doi: 10.1107/S2059798323004254

    Electron density of bound substrates. Initial mF o − DF c density before placing the ligand is shown as a green mesh at 3σ and the final 2 mF o − DF c density is shown as a blue mesh at 1.5σ. ( a , b ) Bound Trp from PDB entry 8cje chain C . ( c , d ) Bound 5-Br-Trp from PDB entry 8cjf chain A . The anomalous signal of bromine in 5-Br-Trp is shown as a yellow mesh (5σ).
    Figure Legend Snippet: Electron density of bound substrates. Initial mF o − DF c density before placing the ligand is shown as a green mesh at 3σ and the final 2 mF o − DF c density is shown as a blue mesh at 1.5σ. ( a , b ) Bound Trp from PDB entry 8cje chain C . ( c , d ) Bound 5-Br-Trp from PDB entry 8cjf chain A . The anomalous signal of bromine in 5-Br-Trp is shown as a yellow mesh (5σ).

    Techniques Used:

    Substrate binding shown in two views. Polar contacts are shown as magenta dashed lines. A salt bridge between Lys587 and the substrate with a distance of longer than 3.5 Å is shown as a cyan dashed line. Only waters connecting the ligand and protein are shown. ( a , b ) Tryptophan (orange C atoms) bound to AetF (yellow C atoms) from PDB entry 8cje chain C . ( c , d ) 5-Br-Trp (dark green C atoms) bound to AetF (green C atoms) from PDB entry 8cjf chain A . Schematic representations of the indole moieties of tryptophan and 5-bromotryptophan with numbered C atoms are added. The grey dashed lines indicate the rotational axis between the binding poses of both ligands.
    Figure Legend Snippet: Substrate binding shown in two views. Polar contacts are shown as magenta dashed lines. A salt bridge between Lys587 and the substrate with a distance of longer than 3.5 Å is shown as a cyan dashed line. Only waters connecting the ligand and protein are shown. ( a , b ) Tryptophan (orange C atoms) bound to AetF (yellow C atoms) from PDB entry 8cje chain C . ( c , d ) 5-Br-Trp (dark green C atoms) bound to AetF (green C atoms) from PDB entry 8cjf chain A . Schematic representations of the indole moieties of tryptophan and 5-bromotryptophan with numbered C atoms are added. The grey dashed lines indicate the rotational axis between the binding poses of both ligands.

    Techniques Used: Binding Assay

    Surface representations of the substrate-binding site with bound Trp (orange C atoms) and 5-Br-Trp (green C atoms). The representations in ( a ) and ( b ) are rotated by 180°. The hydrophobic pocket surrounding the bromine is mostly formed by residues from the insertion in the NADP-binding domain (Leu183, Met217, Val220, Pro250 and Leu254) and by Phe372 from the FAD-binding domain.
    Figure Legend Snippet: Surface representations of the substrate-binding site with bound Trp (orange C atoms) and 5-Br-Trp (green C atoms). The representations in ( a ) and ( b ) are rotated by 180°. The hydrophobic pocket surrounding the bromine is mostly formed by residues from the insertion in the NADP-binding domain (Leu183, Met217, Val220, Pro250 and Leu254) and by Phe372 from the FAD-binding domain.

    Techniques Used: Binding Assay

    Positioning of the substrate relative to the catalytic Lys258 and the possibly catalytic Glu200. ( a ) Superposition of bound Trp (orange C atoms) and 5-Br-Trp (dark green C atoms) with Glu200 and Lys258 from the same structure in yellow and green, respectively. In each case the catalytically preferred C atom points towards the (possibly) catalytic amino acids. ( b ) Bound Trp (orange C atoms) from PDB entry 8cje chain A . Distances to the catalytically preferred position C5 are shown as grey dashed lines and are given in Å.
    Figure Legend Snippet: Positioning of the substrate relative to the catalytic Lys258 and the possibly catalytic Glu200. ( a ) Superposition of bound Trp (orange C atoms) and 5-Br-Trp (dark green C atoms) with Glu200 and Lys258 from the same structure in yellow and green, respectively. In each case the catalytically preferred C atom points towards the (possibly) catalytic amino acids. ( b ) Bound Trp (orange C atoms) from PDB entry 8cje chain A . Distances to the catalytically preferred position C5 are shown as grey dashed lines and are given in Å.

    Techniques Used:

    Related Articles

    Crystallization Assay:

    Article Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF
    Article Snippet: .. Instead of mixing protein and substrate beforehand, we dried 300 nl of 40 mM l-Trp (AppliChem GmbH), saturated 5-Br-Trp (Chem-Impex) or saturated 7-bromotryptophan (7-Br-Trp; provided by Nicolai Montua, OC III, Bielefeld University) on the plate prior to setting up the crystallization plate as described above. ..

    Article Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF
    Article Snippet: .. Instead of mixing protein and substrate beforehand, we dried 300 nl of 40 m M l -Trp (AppliChem GmbH), saturated 5-Br-Trp (Chem-Impex) or saturated 7-bromotryptophan (7-Br-Trp; provided by Nicolai Montua, OC III, Bielefeld University) on the plate prior to setting up the crystallization plate as described above. ..



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    5 br trp chem impex  (Chem Impex International)
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    Chem Impex International 5 br trp chem impex
    Electron density of bound substrates. Initial mF o − DF c density before placing the ligand is shown as a green mesh at 3σ and the final 2 mF o − DF c density is shown as a blue mesh at 1.5σ. ( a , b ) Bound Trp from PDB entry 8cje chain C . ( c , d ) Bound <t>5-Br-Trp</t> from PDB entry 8cjf chain A . The anomalous signal of bromine in 5-Br-Trp is shown as a yellow mesh (5σ).
    5 Br Trp Chem Impex, supplied by Chem Impex International, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/5+br+trp+chem+impex/pmc10306068-114-20-21
    Average 86 stars, based on 1 article reviews
    5 br trp chem impex - by Bioz Stars, 2026-10
    86/100 stars
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    Electron density of bound substrates. Initial mF o − DF c density before placing the ligand is shown as a green mesh at 3σ and the final 2 mF o − DF c density is shown as a blue mesh at 1.5σ. ( a , b ) Bound Trp from PDB entry 8cje chain C . ( c , d ) Bound 5-Br-Trp from PDB entry 8cjf chain A . The anomalous signal of bromine in 5-Br-Trp is shown as a yellow mesh (5σ).

    Journal: Acta Crystallographica. Section D, Structural Biology

    Article Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF

    doi: 10.1107/S2059798323004254

    Figure Lengend Snippet: Electron density of bound substrates. Initial mF o − DF c density before placing the ligand is shown as a green mesh at 3σ and the final 2 mF o − DF c density is shown as a blue mesh at 1.5σ. ( a , b ) Bound Trp from PDB entry 8cje chain C . ( c , d ) Bound 5-Br-Trp from PDB entry 8cjf chain A . The anomalous signal of bromine in 5-Br-Trp is shown as a yellow mesh (5σ).

    Article Snippet: Instead of mixing protein and substrate beforehand, we dried 300 nl of 40 m M l -Trp (AppliChem GmbH), saturated 5-Br-Trp (Chem-Impex) or saturated 7-bromotryptophan (7-Br-Trp; provided by Nicolai Montua, OC III, Bielefeld University) on the plate prior to setting up the crystallization plate as described above.

    Techniques:

    Substrate binding shown in two views. Polar contacts are shown as magenta dashed lines. A salt bridge between Lys587 and the substrate with a distance of longer than 3.5 Å is shown as a cyan dashed line. Only waters connecting the ligand and protein are shown. ( a , b ) Tryptophan (orange C atoms) bound to AetF (yellow C atoms) from PDB entry 8cje chain C . ( c , d ) 5-Br-Trp (dark green C atoms) bound to AetF (green C atoms) from PDB entry 8cjf chain A . Schematic representations of the indole moieties of tryptophan and 5-bromotryptophan with numbered C atoms are added. The grey dashed lines indicate the rotational axis between the binding poses of both ligands.

    Journal: Acta Crystallographica. Section D, Structural Biology

    Article Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF

    doi: 10.1107/S2059798323004254

    Figure Lengend Snippet: Substrate binding shown in two views. Polar contacts are shown as magenta dashed lines. A salt bridge between Lys587 and the substrate with a distance of longer than 3.5 Å is shown as a cyan dashed line. Only waters connecting the ligand and protein are shown. ( a , b ) Tryptophan (orange C atoms) bound to AetF (yellow C atoms) from PDB entry 8cje chain C . ( c , d ) 5-Br-Trp (dark green C atoms) bound to AetF (green C atoms) from PDB entry 8cjf chain A . Schematic representations of the indole moieties of tryptophan and 5-bromotryptophan with numbered C atoms are added. The grey dashed lines indicate the rotational axis between the binding poses of both ligands.

    Article Snippet: Instead of mixing protein and substrate beforehand, we dried 300 nl of 40 m M l -Trp (AppliChem GmbH), saturated 5-Br-Trp (Chem-Impex) or saturated 7-bromotryptophan (7-Br-Trp; provided by Nicolai Montua, OC III, Bielefeld University) on the plate prior to setting up the crystallization plate as described above.

    Techniques: Binding Assay

    Surface representations of the substrate-binding site with bound Trp (orange C atoms) and 5-Br-Trp (green C atoms). The representations in ( a ) and ( b ) are rotated by 180°. The hydrophobic pocket surrounding the bromine is mostly formed by residues from the insertion in the NADP-binding domain (Leu183, Met217, Val220, Pro250 and Leu254) and by Phe372 from the FAD-binding domain.

    Journal: Acta Crystallographica. Section D, Structural Biology

    Article Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF

    doi: 10.1107/S2059798323004254

    Figure Lengend Snippet: Surface representations of the substrate-binding site with bound Trp (orange C atoms) and 5-Br-Trp (green C atoms). The representations in ( a ) and ( b ) are rotated by 180°. The hydrophobic pocket surrounding the bromine is mostly formed by residues from the insertion in the NADP-binding domain (Leu183, Met217, Val220, Pro250 and Leu254) and by Phe372 from the FAD-binding domain.

    Article Snippet: Instead of mixing protein and substrate beforehand, we dried 300 nl of 40 m M l -Trp (AppliChem GmbH), saturated 5-Br-Trp (Chem-Impex) or saturated 7-bromotryptophan (7-Br-Trp; provided by Nicolai Montua, OC III, Bielefeld University) on the plate prior to setting up the crystallization plate as described above.

    Techniques: Binding Assay

    Positioning of the substrate relative to the catalytic Lys258 and the possibly catalytic Glu200. ( a ) Superposition of bound Trp (orange C atoms) and 5-Br-Trp (dark green C atoms) with Glu200 and Lys258 from the same structure in yellow and green, respectively. In each case the catalytically preferred C atom points towards the (possibly) catalytic amino acids. ( b ) Bound Trp (orange C atoms) from PDB entry 8cje chain A . Distances to the catalytically preferred position C5 are shown as grey dashed lines and are given in Å.

    Journal: Acta Crystallographica. Section D, Structural Biology

    Article Title: Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF

    doi: 10.1107/S2059798323004254

    Figure Lengend Snippet: Positioning of the substrate relative to the catalytic Lys258 and the possibly catalytic Glu200. ( a ) Superposition of bound Trp (orange C atoms) and 5-Br-Trp (dark green C atoms) with Glu200 and Lys258 from the same structure in yellow and green, respectively. In each case the catalytically preferred C atom points towards the (possibly) catalytic amino acids. ( b ) Bound Trp (orange C atoms) from PDB entry 8cje chain A . Distances to the catalytically preferred position C5 are shown as grey dashed lines and are given in Å.

    Article Snippet: Instead of mixing protein and substrate beforehand, we dried 300 nl of 40 m M l -Trp (AppliChem GmbH), saturated 5-Br-Trp (Chem-Impex) or saturated 7-bromotryptophan (7-Br-Trp; provided by Nicolai Montua, OC III, Bielefeld University) on the plate prior to setting up the crystallization plate as described above.

    Techniques: