<p><b>a)</b> Changes in the geometry of the protein tertiary structures. Wild type, red; CYP2A6*15, green; CYP2A6*16, blue; CYP2A6*21, black; CYP2A6*22, magenta; <b>b)</b> Superimposition of the wild type and mutant structures. Yellow circle indicates the binding site.</p
<p>(A) Charmm_mini; (B) Charmm_ave; (C) Charmm_706ps. In the cartoon representations, the green and ...
<p>(A) and (B) Structure of the Wild Type showing polar and charged inter protein interactions respe...
<p>*34 has a single mutation at R296C (purple) on helix I and distal to the active site. *17-2 has t...
<p><b>a)</b> Space-filling representation of amino acid residues forming the CYP2A6 active sites. a1...
<p>3D structure was predicted at Protein Homology/analogY Recognition Engine (PhyreEngine) from the ...
(a) Overview of CYP1B1 wild type protein in ribbon-presentation (b-l) In-silico protein prediction r...
<p><b>(A) Wild-type enzyme; (B) A269K/S187D mutant; (C) S187D/N188T mutant; D) A269K/S187D/N188T mut...
<p>The mutant backbone is basically unaltered from wild type (Cα rmsd 0.9 Å). (a) Structural compari...
<p>A) Wild type protein structure with an intact disulphide bridge showing position of the mutated r...
<p>N.D.: not detectable.</p><p>a) RMSFs around C helices are large.</p><p>b) RMSFs around G helices ...
<p>(A) The whole complex structure. CYP2B6.1 is shown by ribbon, heme and AM are shown by ball-and-s...
<p>The five columns correspond to ΔFI<sub>n</sub>, ΔCC<sub>n</sub> with respect to Glu35, ΔCC<sub>n<...
<p>Amino acid change at 690th position for DPP3 leads to the structural changes at the C-terminus (i...
<p>Close-up images of the substrate binding sites for the ten enzymes in our benchmark with known sp...
<p>A) Superposition of wild type (orange) and H234A (magenta) dimers using only A chain for structur...
<p>(A) Charmm_mini; (B) Charmm_ave; (C) Charmm_706ps. In the cartoon representations, the green and ...
<p>(A) and (B) Structure of the Wild Type showing polar and charged inter protein interactions respe...
<p>*34 has a single mutation at R296C (purple) on helix I and distal to the active site. *17-2 has t...
<p><b>a)</b> Space-filling representation of amino acid residues forming the CYP2A6 active sites. a1...
<p>3D structure was predicted at Protein Homology/analogY Recognition Engine (PhyreEngine) from the ...
(a) Overview of CYP1B1 wild type protein in ribbon-presentation (b-l) In-silico protein prediction r...
<p><b>(A) Wild-type enzyme; (B) A269K/S187D mutant; (C) S187D/N188T mutant; D) A269K/S187D/N188T mut...
<p>The mutant backbone is basically unaltered from wild type (Cα rmsd 0.9 Å). (a) Structural compari...
<p>A) Wild type protein structure with an intact disulphide bridge showing position of the mutated r...
<p>N.D.: not detectable.</p><p>a) RMSFs around C helices are large.</p><p>b) RMSFs around G helices ...
<p>(A) The whole complex structure. CYP2B6.1 is shown by ribbon, heme and AM are shown by ball-and-s...
<p>The five columns correspond to ΔFI<sub>n</sub>, ΔCC<sub>n</sub> with respect to Glu35, ΔCC<sub>n<...
<p>Amino acid change at 690th position for DPP3 leads to the structural changes at the C-terminus (i...
<p>Close-up images of the substrate binding sites for the ten enzymes in our benchmark with known sp...
<p>A) Superposition of wild type (orange) and H234A (magenta) dimers using only A chain for structur...
<p>(A) Charmm_mini; (B) Charmm_ave; (C) Charmm_706ps. In the cartoon representations, the green and ...
<p>(A) and (B) Structure of the Wild Type showing polar and charged inter protein interactions respe...
<p>*34 has a single mutation at R296C (purple) on helix I and distal to the active site. *17-2 has t...