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==<p style="font-size:x-large;"><b>NAPase</b></p>== | ==<p style="font-size:x-large;"><b>NAPase</b></p>== | ||
{{STRUCTURE_2oua | PDB=2oua | SCENE= }} | |||
Nocardiopsis alba Protease A, or NAPase, is an acid-resistant homolog of <i>alpha</i>-lytic protease. As such, NAPase and <i>a</i>lp 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. | |||
Revision as of 16:06, 22 June 2010
Please do NOT make changes to this sandbox. Sandboxes 10-30 are currently reserved by Prof. Sheila Jaswal at Amherst College.
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.