<p>(A) Sequence alignment of model WP_003403850.1 and template PDB_ID: 4PZ9:B indicating the catalytic residues (#). In all the pair-wise sequence alignments, identical residues are indicated in gray shaded regions, deletions in the template sequence is indicated as dots in brown shaded region, deletions in the query sequence is indicated as dots in yellow shaded region. (B) Structure alignment of model (green) and template (pink).</p
<p>(A) Docked model of pNPG in the active site of BglB showing established catalytic residues (navy)...
<p>(A) Aligned homological models of PORA (blue), PORB (yellow) and PORC (green). Structures of pair...
<p>IRS1 (PDB ID: 1QQG), TAPP1 (PDB ID: 1EAZ), Myosin X (PDB ID: 3TFM) and DAPP1 (PDB ID: 1FAO). The ...
<p>(A) Sequence alignment of model ABL03629.1 and template PDB _ID: 2DSK:A indicating the catalytic ...
<p>(A) Sequence alignment of model CPR01223.1 and template PDB _ID: 4K1C:B. (B) Structure alignment ...
<p>(A) Sequence alignment of model AGC62230.1 and template PDB _ID: 4L0E:A indicating consensus heme...
<p>(<b>A</b>) <b>Sequence alignment of MtSerB2</b> with sequences of Phosphoserine phosphatases from...
<p>(A) Sequence alignment of <i>S. cerevisiae</i> α-glucosidase (represented as YEAST) with <i>B. ce...
<p>Numbering indicates the position of the first and last residue in each aligned sequence. Proteins...
<p>(<b>a</b>) The catalytic domain of CNA is highly conserved around the β12 and β13 connection in P...
<p>The cartoon representation of protease domain of model VCO395_1035 (magenta) aligned with templat...
<p><b>(A)</b> Schematic representation of the domain structure. The predicted transmembrane helices ...
<p>(a) SMARCAD1, (b) GSG2, (c) NUP35, (d) NEK5, (e) KIF23 and (f) CEP170. MSA illustrates the conser...
<p>Three domains of PgdS, the NlpC/P60 catalytic domains of LytF, LytE and CwlS from <i>B</i>. <i>su...
<p>Green stars indicate the residues of the catalytic triad; conserved residues are shaded in red. B...
<p>(A) Docked model of pNPG in the active site of BglB showing established catalytic residues (navy)...
<p>(A) Aligned homological models of PORA (blue), PORB (yellow) and PORC (green). Structures of pair...
<p>IRS1 (PDB ID: 1QQG), TAPP1 (PDB ID: 1EAZ), Myosin X (PDB ID: 3TFM) and DAPP1 (PDB ID: 1FAO). The ...
<p>(A) Sequence alignment of model ABL03629.1 and template PDB _ID: 2DSK:A indicating the catalytic ...
<p>(A) Sequence alignment of model CPR01223.1 and template PDB _ID: 4K1C:B. (B) Structure alignment ...
<p>(A) Sequence alignment of model AGC62230.1 and template PDB _ID: 4L0E:A indicating consensus heme...
<p>(<b>A</b>) <b>Sequence alignment of MtSerB2</b> with sequences of Phosphoserine phosphatases from...
<p>(A) Sequence alignment of <i>S. cerevisiae</i> α-glucosidase (represented as YEAST) with <i>B. ce...
<p>Numbering indicates the position of the first and last residue in each aligned sequence. Proteins...
<p>(<b>a</b>) The catalytic domain of CNA is highly conserved around the β12 and β13 connection in P...
<p>The cartoon representation of protease domain of model VCO395_1035 (magenta) aligned with templat...
<p><b>(A)</b> Schematic representation of the domain structure. The predicted transmembrane helices ...
<p>(a) SMARCAD1, (b) GSG2, (c) NUP35, (d) NEK5, (e) KIF23 and (f) CEP170. MSA illustrates the conser...
<p>Three domains of PgdS, the NlpC/P60 catalytic domains of LytF, LytE and CwlS from <i>B</i>. <i>su...
<p>Green stars indicate the residues of the catalytic triad; conserved residues are shaded in red. B...
<p>(A) Docked model of pNPG in the active site of BglB showing established catalytic residues (navy)...
<p>(A) Aligned homological models of PORA (blue), PORB (yellow) and PORC (green). Structures of pair...
<p>IRS1 (PDB ID: 1QQG), TAPP1 (PDB ID: 1EAZ), Myosin X (PDB ID: 3TFM) and DAPP1 (PDB ID: 1FAO). The ...