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Schrodinger LLC pymol molecular graphics system version 3.0
Pymol Molecular Graphics System Version 3.0, supplied by Schrodinger LLC, 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/graphical+visualisations/pymol+molecular+graphics+system+version+2+0/pmc11708228-78-20-26
Average 90 stars, based on 1 article reviews
pymol molecular graphics system version 3.0 - by Bioz Stars, 2026-11
90/100 stars

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Related Articles

other:

Article Title: Hepatoprotective and Nephroprotective Effects of Leea guineensis Leaf Extract Against Paracetamol-Induced Toxicity: Combined Mouse Model-Integrated in Silico Evidence.
Article Snippet: The PyMol Molecular Graphics version 1.7.4 Schrodinger LLC, downloaded from pymol.org on 25th September, 2023, was used to convert the compounds in SDF format to PDB files.

Article Title:
Article Snippet: [21] Schrodinger, LLC, The PyMOL Molecular Graphics System, Version 2.4.1.

Article Title: Supporting Information Metal-Free Arylation of Benzothiophenes at C4 by Activation as their Benzothiophene S-Oxides
Article Snippet: The PyMOL Molecular Graphics System, version 2.0.7, Schrodinger, LLC.

Article Title: Computational Elucidation of Sterol Recognition by SREBP Cleavage Activatory Protein.
Article Snippet: Rep 2020, 10, 16903. (26) Schrodinger, LLC The PyMOL Molecular Graphics System, version 1.8; 2015. (27) Abraham, M. J.; et al. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers.

Article Title: Supporting Information for Transient interactions modulate affinity of NF-κB transcription factors for DNA
Article Snippet: Schrodinger, LLC (2015) The PyMOL Molecular Graphics System, Version 2.0.

Article Title: Structural basis for sirtuin 2 activity and modulation: Current state and opportunities
Article Snippet: Created with PyMOL(TM) Molecular Graphics System, Version 2.5.0., Schrodinger, LLC.



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Active site of K69A T. brucei ODC in complex with DFMO. The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom). In reference 7, the N terminus of recombinant T. brucei ODC corresponds to the 21st residue of intact ODC (Fig. ​(Fig.3).3). Residues (V62, T63, P64, D72, and T359) which correspond to the residues mutated in this study and were identified as functionally important for substrate specificity in S. ruminantium LDC are purple and violet. The atoms of PLP are yellow, the atoms of DFMO are green, A69 and C360 are orange, and Y389 and F397, which cradle the aliphatic portion of DFMO, are brown. R277, D332, and D361 are also shown, and nitrogen and oxygen atoms of these residues are blue and red, respectively. The asterisked residues belong to the other subunit of the dimer.
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Active site of K69A T. brucei ODC in complex with DFMO. The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom). In reference 7, the N terminus of recombinant T. brucei ODC corresponds to the 21st residue of intact ODC (Fig. ​(Fig.3).3). Residues (V62, T63, P64, D72, and T359) which correspond to the residues mutated in this study and were identified as functionally important for substrate specificity in S. ruminantium LDC are purple and violet. The atoms of PLP are yellow, the atoms of DFMO are green, A69 and C360 are orange, and Y389 and F397, which cradle the aliphatic portion of DFMO, are brown. R277, D332, and D361 are also shown, and nitrogen and oxygen atoms of these residues are blue and red, respectively. The asterisked residues belong to the other subunit of the dimer.

Journal:

Article Title: Gene Cloning and Molecular Characterization of Lysine Decarboxylase from Selenomonas ruminantium Delineate Its Evolutionary Relationship to Ornithine Decarboxylases from Eukaryotes

doi:

Figure Lengend Snippet: Active site of K69A T. brucei ODC in complex with DFMO. The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom). In reference 7, the N terminus of recombinant T. brucei ODC corresponds to the 21st residue of intact ODC (Fig. ​(Fig.3).3). Residues (V62, T63, P64, D72, and T359) which correspond to the residues mutated in this study and were identified as functionally important for substrate specificity in S. ruminantium LDC are purple and violet. The atoms of PLP are yellow, the atoms of DFMO are green, A69 and C360 are orange, and Y389 and F397, which cradle the aliphatic portion of DFMO, are brown. R277, D332, and D361 are also shown, and nitrogen and oxygen atoms of these residues are blue and red, respectively. The asterisked residues belong to the other subunit of the dimer.

Article Snippet: The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom).

Techniques: Recombinant