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BioSolveIT GmbH seesar
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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MedCalc Software Ltd version 13.0 for windows
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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SYSTAT sigmaplot for windows
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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STATA Corporation stata mp for windows
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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SSPS Inc spss windows, version 13.0
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
Spss Windows, Version 13.0, supplied by SSPS Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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BioSolveIT GmbH flexx feature of seesar version 13.0
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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BioSolveIT GmbH seesar version 13.0
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
Seesar Version 13.0, 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/de+windows+versi%C3%B3n+13%2E0/seesar+version+12+1+0/pmc10993276-87-25-29
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seesar version 13.0 - by Bioz Stars, 2026-09
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BioSolveIT GmbH seesar software
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
Seesar Software, 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/de+windows+versi%C3%B3n+13%2E0/seesar+software/pmc11767819-123-5-9
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StatsDirect ltd statsdirect version 2.4.5
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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MedCalc Software Ltd windows, version 13.0.2
(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: <t>Haloarcura</t> <t>marismortui</t> , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with <t>SeeSAR</t> software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.
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Image Search Results


(A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: Haloarcura marismortui , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with SeeSAR software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.

Journal: RSC Chemical Biology

Article Title: Biotransformation-coupled mutasynthesis for the generation of novel pristinamycin derivatives by engineering the phenylglycine residue

doi: 10.1039/d3cb00143a

Figure Lengend Snippet: (A) Structure of quinupristin (2) and illustration of the network of hydrogen bonds and lipophilic interactions with bacterial 23S rRNA bases in the 50S subunit of the bacterial ribosomes (green: E. coli , PBD: 4U26 , red: Deinococcus radiodurans , PBD: 1SM1, Black: Haloarcura marismortui , PBD: 1YJW . Illustration of docked pristinamycin (1) into the binding pocket at the 23S rRNA of E. coli (B), H. marismortui (C) and D. radiodurans (D) in comparison to quinupristin (2, depicted in red) prepared with SeeSAR software version 13.0.1 ( https://www.biosolveit.de/SeeSAR ). Colored spheres around atoms indicate positive (green) or negative (red) contributions to the overall binding affinity based on ligand–target interactions as well as desolvatization energies.

Article Snippet: However, as no co-crystal structure of 1 with the bacterial ribosome is available, we have performed a virtual docking of pristinamycin I (1) into the binding pocket of quinupristin (2) at the ribosome based on the three available co-crystal structure with the ribosome of E. coli (PDB: 4U26 ), D. radiodurans (PDB: 1MS1 ), and H. marismortui (PBD: 1YJW ) using the software SeeSAR (SeeSAR version 13.0.1; BioSolveIT GmbH, Sankt Augustin, Germany, 2023, www.biosolveit.de/SeeSAR).

Techniques: Binding Assay, Comparison, Software