<p>Comparison of the catalytic triad residues and active site arrangement of active and inactive form of the protease domain.</p
Abstract- We propose a novel method for defining the exclusive and exhaustive table of serine protea...
<p>Comparison of <i>E. coli</i> PBP4 (coloured yellow, active site serine S62, only selected residue...
Relative amount of cleavage sites assigned to enzymes identified by Proteasix.</p
<p>A. Substrate binding site of inactive form of protease domain modeled using template 3STI. B. Sub...
It Is well established that a sequence template along with the database is a powerful tool for iden...
<p>RMSD values for each catalytic residue are shown for the entire residue (a, b, c) and the corresp...
<p>Eukaryotic proteases (3EST, 1TON, 3RP2, 5CHA) are in blue, prokaryotic (1SGT, 2SGA, 3SGB, 2ALP) i...
Backgound: Serine protease activity is critical for many biological processes and has arisen indepen...
<p>(a) Both model structures of HCV-4a (blue) and HCV-3a (red) are superimposed onto the template st...
<p>(a) The N-terminal protease domain of N<sup>pro</sup>. The catalytic dyad (Cys69 and His49) is sh...
The Asp–His–Ser triad of serine proteases has been regarded, in the present study, as an independent...
<p>In each panel, from the left to right, are the assignments at each position for secondary structu...
<p>A: Detailed view of the active site of TbOPB in the open and closed state. Open and closed states...
The Asp-His-Ser triad of serine proteases has been regarded, in the present study, as an independent...
<p>The cartoon representation of protease domain of model VCO395_1035 (magenta) aligned with templat...
Abstract- We propose a novel method for defining the exclusive and exhaustive table of serine protea...
<p>Comparison of <i>E. coli</i> PBP4 (coloured yellow, active site serine S62, only selected residue...
Relative amount of cleavage sites assigned to enzymes identified by Proteasix.</p
<p>A. Substrate binding site of inactive form of protease domain modeled using template 3STI. B. Sub...
It Is well established that a sequence template along with the database is a powerful tool for iden...
<p>RMSD values for each catalytic residue are shown for the entire residue (a, b, c) and the corresp...
<p>Eukaryotic proteases (3EST, 1TON, 3RP2, 5CHA) are in blue, prokaryotic (1SGT, 2SGA, 3SGB, 2ALP) i...
Backgound: Serine protease activity is critical for many biological processes and has arisen indepen...
<p>(a) Both model structures of HCV-4a (blue) and HCV-3a (red) are superimposed onto the template st...
<p>(a) The N-terminal protease domain of N<sup>pro</sup>. The catalytic dyad (Cys69 and His49) is sh...
The Asp–His–Ser triad of serine proteases has been regarded, in the present study, as an independent...
<p>In each panel, from the left to right, are the assignments at each position for secondary structu...
<p>A: Detailed view of the active site of TbOPB in the open and closed state. Open and closed states...
The Asp-His-Ser triad of serine proteases has been regarded, in the present study, as an independent...
<p>The cartoon representation of protease domain of model VCO395_1035 (magenta) aligned with templat...
Abstract- We propose a novel method for defining the exclusive and exhaustive table of serine protea...
<p>Comparison of <i>E. coli</i> PBP4 (coloured yellow, active site serine S62, only selected residue...
Relative amount of cleavage sites assigned to enzymes identified by Proteasix.</p
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