Ann Taylor Sandbox 118
From Proteopedia
(→This is a placeholder) |
|||
| Line 6: | Line 6: | ||
<applet load="2ptc" size="350" color="white" frame="true" align="right" spinBox="true" | <applet load="2ptc" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="Trypsin BPT1 complex" /> | caption="Trypsin BPT1 complex" /> | ||
| + | |||
| + | ==Trypsin-BPTI complex== | ||
| + | The trypsin backbone is shown in pink and the trypsin inhibitor, BPTI, in yellow (PDB code [[2ptc]]). The <scene name='Serine_Protease/Active_site/3'>active site</scene> residues [Ser195-His57-Asp102-Ser214] are shown in green, the disulfide bond between residues 14-38 is shown in yellow and the Lys 15 sidechain at the specificity site in pink. | ||
Revision as of 23:38, 20 February 2011
Thrombin
Thrombin is a "trypsin-like" serine protease. Its structure (PDB code 1ppb) is shown here with a peptide chloroketone inhibitor (PPACK). The thrombin A chain (cleaved N terminal fragement) is shown in cyan and the B chain is shown in red. The is made up of a catalytic triad of Ser195, His57 and Asp102, backed up by Ser214. The peptide chloroketone inhibitor (PPACK) is shown in purple. A closeup shows the at which the sidechain of Asp194 makes a salt link with the N-terminus at residue 16, newly formed when the A chain is cleaved in the zymogen-to-enzyme activation process. The specificity pocket is on one side of the throat of the domain 2 beta barrel, and the activation site is close next to it.
The B chain consists of . As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel. The specificity pocket (here filled with the Lys sidechain of the PPACK inhibitor) is in one side of the throat of the domain 2beta barrel, and the activation site is close next to it.
|
Trypsin-BPTI complex
The trypsin backbone is shown in pink and the trypsin inhibitor, BPTI, in yellow (PDB code 2ptc). The residues [Ser195-His57-Asp102-Ser214] are shown in green, the disulfide bond between residues 14-38 is shown in yellow and the Lys 15 sidechain at the specificity site in pink.
Gilman suc-AAPK-trypssin
suc-AAPK-trypssin is a serine protease in the acyl enzyme state. Structure 118 is the form of the acyl enzyme in which tetrahedral intermediate has collapsed and after the first peptide bond has been cleaved. Only one half of the enzyme remains in the active site.
Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure.
