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| Reference: |
Yin J, Niu C, Cherney MM, Zhang J, Huitema C, Eltis LD, Vederas JC, James MNA mechanistic view of enzyme inhibition and peptide hydrolysis in the active site of the SARS-CoV 3C-like peptidaseJ. Mol. Biol. v371, p.1060-1074The 3C-like main peptidase 3CL(pro) is a viral polyprotein processing enzyme essential for the viability of the Severe Acute Respiratory Syndrome coronavirus (SARS-CoV). While it is generalized that 3CL(pro) and the structurally related 3C(pro) viral peptidases cleave their substrates via a mechanism similar to that underlying the peptide hydrolysis by chymotrypsin-like serine proteinases (CLSPs), some of the hypothesized key intermediates have not been structurally characterized....
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| Description: |
A Mechanistic View Of Enzyme Inhibition And Peptide Hydrolysis In The Active Site Of The Sars-Cov 3c-Like Peptidase. |
| Deposition: |
2007/6/4   |
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| Taxonomy: |
Chain I:(unassigned)
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VAST related structures have been calculated separately for individual protein chains and 3d domains present in this structure. To see the related structure list for each choose a chain or 3d domain from the table below.
| Chain ID |
Domains |
Residue Range |
No. of Neighbors |
|---|
| [A] |
entire chain |
1 - 306 |
N/A (in progress) |
| [A] |
domain 1 |
1 - 189 |
N/A (in progress) |
| [A] |
domain 2 |
190 - 306 |
N/A (in progress) |
| [I] |
entire chain |
1 - 4 |
N/A (in progress) |
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| Click to view a graphical summary of the protein chains and domains present in this entry. |
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