Sandbox Reserved 321: Difference between revisions
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by Kelly Hrywkiw | by Kelly Hrywkiw | ||
{{STRUCTURE_2h9i | PDB=2h9i | SCENE= }} | {{STRUCTURE_2h9i | PDB=2h9i | SCENE= }} | ||
[[Image: | [[Image:Stero veiw.png|thumb|left|upright=2.5|alt=Secondary Structure Succession of InhA. Secondary structure residues are ordered from blue to red.|Stero view of the homotetramer structure of InhA with secondary structure succession outlined]] | ||
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<scene name='Sandbox_Reserved_321/Substructure_2/1'>Substructure 2</scene> contains the c-terminal region of the molecule and consists of a small β strand <scene name='Sandbox_Reserved_321/B-7/1'>(B-7)</scene>, and two α helices <scene name='Sandbox_Reserved_321/A-6_and_a-7/1'>(A-6 and A-7)</scene> which are connected by a short five residue loop<ref name ="making drugs for inhA"/>. The C-terminal domain consits of two other α helices <scene name='Sandbox_Reserved_321/A-8_and_a-9/1'>(A-8 and A-9)</scene><ref name ="making drugs for inhA"/>. | <scene name='Sandbox_Reserved_321/Substructure_2/1'>Substructure 2</scene> contains the c-terminal region of the molecule and consists of a small β strand <scene name='Sandbox_Reserved_321/B-7/1'>(B-7)</scene>, and two α helices <scene name='Sandbox_Reserved_321/A-6_and_a-7/1'>(A-6 and A-7)</scene> which are connected by a short five residue loop<ref name ="making drugs for inhA"/>. The C-terminal domain consits of two other α helices <scene name='Sandbox_Reserved_321/A-8_and_a-9/1'>(A-8 and A-9)</scene><ref name ="making drugs for inhA"/>. | ||
== | ==Hydrophobic Binding Pocket== | ||
InhA contains a <scene name='Sandbox_Reserved_321/Hydrophobic_binding_pocket/1'>hydrophobic pocket</scene>where ligands bind to a higly conserved binding site<ref name ="mech of thioamide drug action"/>. The site is lined with the hydrophobic residues tyrosine 158 (Y158), phenylalanine 149 (F149) methionine 199 (M199, trypotophan 222 (W222), leucine 218 (K218), methionine 161 (M161), and proline 193 (P193)<ref name ="mech of thioamide drug action"/>. The fatty acyl binding site is also located in the hydrophobic pocket of InhA and consists primairly of the substrate binding loop <scene name='Sandbox_Reserved_321/Substrate_binding_lopp/1'>(residues 196-219)</scene><ref name ="Fatty acyl in InhA">PMID:10336454</ref>. | InhA contains a <scene name='Sandbox_Reserved_321/Hydrophobic_binding_pocket/1'>hydrophobic pocket</scene>where ligands bind to a higly conserved binding site<ref name ="mech of thioamide drug action"/>. The site is lined with the hydrophobic residues tyrosine 158 (Y158), phenylalanine 149 (F149) methionine 199 (M199, trypotophan 222 (W222), leucine 218 (K218), methionine 161 (M161), and proline 193 (P193)<ref name ="mech of thioamide drug action"/>. The fatty acyl binding site is also located in the hydrophobic pocket of InhA and consists primairly of the substrate binding loop <scene name='Sandbox_Reserved_321/Substrate_binding_lopp/1'>(residues 196-219)</scene><ref name ="Fatty acyl in InhA">PMID:10336454</ref>. | ||
