<p>Left, BglA dimer with the putative active site outlined in a gray box. Right, close up of the active site with glucose-6-phosphate modeled based of the position of the sulfate ion from crystallization. Active site residues are depicted as ball-and-stick. Putative hydrogen bonds to the substrate are drawn as dashed lines.</p
<p>(<b>a</b>,<b>b</b>) Proposed active site of PduL with relevant residues shown as sticks in atom c...
A: reactions of (C30)6 with Tgl. We propose that the (C30)6 hexamer acts both as a Q and K donor and...
Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the first and rate-determining step in the Pento...
<p>Left, the YghZ tetramer viewed along the four-fold axis. Putative active site residues are depict...
<p><b>Figure S2. Docking of substrates into the active site representation of LigW_Sp or LigW2_Sp</b...
<p>Left, the pGI dimer. Right, close -up view of the active site with putative active site residues ...
<p>(A) Overview of the entire active site region, shown for chain A of the native protein. EcMenH is...
<p>(A) Amino acid residues and bound substrate are shown in thin stick and ball-stick forms, respect...
<p>The amino acid residues are shown in thin stick form and bound substrate is shown in ball-stick f...
<p>Glycosidases are represented as gray surfaces with catalytic clefts colored in blue and catalytic...
Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the first and rate-limiting step of the pentose ...
<p>The surface of the protein is colored based on the electrostatic potential. NAMN (orange) and res...
<p>The initial and final locations of each binding residue are shown in yellow and green, respective...
<p>View of the active site with NADH bound in the optimized position found by docking as described i...
<p>(A) A D-lysine molecule from the crystallisation condition is bound within the active site of mol...
<p>(<b>a</b>,<b>b</b>) Proposed active site of PduL with relevant residues shown as sticks in atom c...
A: reactions of (C30)6 with Tgl. We propose that the (C30)6 hexamer acts both as a Q and K donor and...
Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the first and rate-determining step in the Pento...
<p>Left, the YghZ tetramer viewed along the four-fold axis. Putative active site residues are depict...
<p><b>Figure S2. Docking of substrates into the active site representation of LigW_Sp or LigW2_Sp</b...
<p>Left, the pGI dimer. Right, close -up view of the active site with putative active site residues ...
<p>(A) Overview of the entire active site region, shown for chain A of the native protein. EcMenH is...
<p>(A) Amino acid residues and bound substrate are shown in thin stick and ball-stick forms, respect...
<p>The amino acid residues are shown in thin stick form and bound substrate is shown in ball-stick f...
<p>Glycosidases are represented as gray surfaces with catalytic clefts colored in blue and catalytic...
Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the first and rate-limiting step of the pentose ...
<p>The surface of the protein is colored based on the electrostatic potential. NAMN (orange) and res...
<p>The initial and final locations of each binding residue are shown in yellow and green, respective...
<p>View of the active site with NADH bound in the optimized position found by docking as described i...
<p>(A) A D-lysine molecule from the crystallisation condition is bound within the active site of mol...
<p>(<b>a</b>,<b>b</b>) Proposed active site of PduL with relevant residues shown as sticks in atom c...
A: reactions of (C30)6 with Tgl. We propose that the (C30)6 hexamer acts both as a Q and K donor and...
Glucose-6-phosphate dehydrogenase (G6PDH) catalyzes the first and rate-determining step in the Pento...