1a1q
From Proteopedia
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| - | [[Image:1a1q.gif|left|200px]] | + | [[Image:1a1q.gif|left|200px]] |
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| - | '''HEPATITIS C VIRUS NS3 PROTEINASE''' | + | {{Structure |
| + | |PDB= 1a1q |SIZE=350|CAPTION= <scene name='initialview01'>1a1q</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11103 Hepatitis C virus]) | ||
| + | }} | ||
| + | |||
| + | '''HEPATITIS C VIRUS NS3 PROTEINASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A1Q is a [ | + | 1A1Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1Q OCA]. |
==Reference== | ==Reference== | ||
| - | The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site., Love RA, Parge HE, Wickersham JA, Hostomsky Z, Habuka N, Moomaw EW, Adachi T, Hostomska Z, Cell. 1996 Oct 18;87(2):331-42. PMID:[http:// | + | The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site., Love RA, Parge HE, Wickersham JA, Hostomsky Z, Habuka N, Moomaw EW, Adachi T, Hostomska Z, Cell. 1996 Oct 18;87(2):331-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8861916 8861916] |
[[Category: Hepatitis c virus]] | [[Category: Hepatitis c virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:39 2008'' |
Revision as of 07:51, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Gene: | CDNA (Hepatitis C virus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HEPATITIS C VIRUS NS3 PROTEINASE
Overview
During replication of hepatitis C virus (HCV), the final steps of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of nonstructural protein 3. The structure of NS3 proteinase from HCV BK strain was determined by X-ray crystallography at 2.4 angstrom resolution. NS3P folds as a trypsin-like proteinase with two beta barrels and a catalytic triad of His-57, Asp-81, Ser-139. The structure has a substrate-binding site consistent with the cleavage specificity of the enzyme. Novel features include a structural zinc-binding site and a long N-terminus that interacts with neighboring molecules by binding to a hydrophobic surface patch.
About this Structure
1A1Q is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.
Reference
The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site., Love RA, Parge HE, Wickersham JA, Hostomsky Z, Habuka N, Moomaw EW, Adachi T, Hostomska Z, Cell. 1996 Oct 18;87(2):331-42. PMID:8861916
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