Sandbox 11
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NAPase
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| 2oua, resolution 1.85Å () | |||||||||
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| Ligands: | , , , | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Nocardiopsis alba Protease A, or NAPase, is an acid-resistant homolog of alpha-lytic protease. As such, NAPase and alp are both kinetically stable proteases, meaning it is the large barrier to unfolding that keeps this protease in its folded, active state. This is different from most other proteins, which stay in their folded, or native, state because of the energy difference between their native and unfolded states, with the native state being lower in energy.
The NAPase molecule provided shows two NAPase molecules that are mirror images, so here is just . NAPase, along with the rest of the trypsin family, has an active site that consists of the "catalytic triad." This is made up of three amino acid residues (H57, D102, and S195) that play a major role in binding the substrate and catalyzing proteolysis.
One of the major features of NAPase is that each protease has two domains, an N domain and a C domain. In this , one can see the N domain (red, orange, yellow), so-called because it contains the N-terminal amino acid, is connected covalently through the protein to the C domain (green, blue, violet). The horizontal axis of this scene is the main dividing line between the domains, with few chains crossing the barrier.