Ribokinase: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
Upon forming a ternary complex of RK, ribose and nucleotide the RK dimer changes its open form to a closed one. The ribose substrate is seen between a small β-sheel domain and the concave side of the central β sheet<ref>PMID:30822455</ref>. <scene name='91/915829/Cv/3'>The ribose binding site</scene> is lined with charged residues. | Upon forming a ternary complex of RK, ribose and nucleotide the RK dimer changes its open form to a closed one. The ribose substrate is seen between a small β-sheel domain and the concave side of the central β sheet<ref>PMID:30822455</ref>. <scene name='91/915829/Cv/3'>The ribose binding site</scene> is lined with charged residues. Water molecules are shown as red spheres. The <scene name='91/915829/Cv/6'>ATP binding site</scene> is surrounded by hydrophobic residues. <scene name='91/915829/Cv/7'>Na coordination site</scene>. | ||
==Ribokinase 3D structures== | ==Ribokinase 3D structures== | ||