<p>Distance graph (in left) of catalytic sulfide atoms for electron transfer in AtNTR_CC (blue) between Cys153:S (in subunit B) and Cys387–Cys390:S-S (in subunit A) and for that in AtNTR_AC (red) between Cys147:S (in subunit A) and Cys384–Cys387:S-S (in subunit B). In the right panel, the key catalytic residues are represented by stick model.</p
Structural informatics of conservation of inter-catalytic residue atom distances A- The RMSD of each...
<p>The active site is depicted in a ball-and-stick representation (C = black, O = red, N = blue, H =...
<p>A) Variation of the atomic distance d(R/H681, CA - H679’, O) as a characteristic proximal inter-s...
<p>Distance between sulfur atoms of the free thiol Cys560 in the representative C583S simulation and...
The process of deducing the catalytic mechanism of an enzyme from its structure is highly complex an...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is surface represented and...
<p>Distance between the catalytic Ser195 residue of thrombin and the P1 residue carbonyl carbon in t...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is represented by ribbons ...
<p>The methodology of the analyses performed is described in the <a href="http://www.plosone.org/art...
<p>Unique disulfide bond near the active site: unique disulfide bond Cys90 – Cys126 next to the cata...
CsdA cysteine desulfurase (the sulfur donor) and the CsdE sulfur acceptor are involved in biological...
An analysis of the geometry of binding of metal ions by cysteine and methionine residues in protein ...
<p>(<b>A</b>) The time course of the distance between the two active sites of hPDI in Sim 3 (blue) a...
<p>The backbone of GLA is shown as a line. The atoms involved in the formation of a disulfide bond (...
<p>A.) Subunit A. B.) Subunit B. The 2Fobs – Fcalc electron density map, displayed around the cystei...
Structural informatics of conservation of inter-catalytic residue atom distances A- The RMSD of each...
<p>The active site is depicted in a ball-and-stick representation (C = black, O = red, N = blue, H =...
<p>A) Variation of the atomic distance d(R/H681, CA - H679’, O) as a characteristic proximal inter-s...
<p>Distance between sulfur atoms of the free thiol Cys560 in the representative C583S simulation and...
The process of deducing the catalytic mechanism of an enzyme from its structure is highly complex an...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is surface represented and...
<p>Distance between the catalytic Ser195 residue of thrombin and the P1 residue carbonyl carbon in t...
<p>The 3D<b>-</b>EP24.15 structure focusing S-glutathiolated Cys residues is represented by ribbons ...
<p>The methodology of the analyses performed is described in the <a href="http://www.plosone.org/art...
<p>Unique disulfide bond near the active site: unique disulfide bond Cys90 – Cys126 next to the cata...
CsdA cysteine desulfurase (the sulfur donor) and the CsdE sulfur acceptor are involved in biological...
An analysis of the geometry of binding of metal ions by cysteine and methionine residues in protein ...
<p>(<b>A</b>) The time course of the distance between the two active sites of hPDI in Sim 3 (blue) a...
<p>The backbone of GLA is shown as a line. The atoms involved in the formation of a disulfide bond (...
<p>A.) Subunit A. B.) Subunit B. The 2Fobs – Fcalc electron density map, displayed around the cystei...
Structural informatics of conservation of inter-catalytic residue atom distances A- The RMSD of each...
<p>The active site is depicted in a ball-and-stick representation (C = black, O = red, N = blue, H =...
<p>A) Variation of the atomic distance d(R/H681, CA - H679’, O) as a characteristic proximal inter-s...