1a1q
From Proteopedia
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|PDB= 1a1q |SIZE=350|CAPTION= <scene name='initialview01'>1a1q</scene>, resolution 2.4Å | |PDB= 1a1q |SIZE=350|CAPTION= <scene name='initialview01'>1a1q</scene>, resolution 2.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11103 Hepatitis C virus]) | |GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11103 Hepatitis C virus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a1q OCA], [http://www.ebi.ac.uk/pdbsum/1a1q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a1q RCSB]</span> | ||
}} | }} | ||
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[[Category: Parge, H E.]] | [[Category: Parge, H E.]] | ||
[[Category: Wickersham, J A.]] | [[Category: Wickersham, J A.]] | ||
| - | [[Category: ZN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:16 2008'' |
Revision as of 15:31, 30 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CDNA (Hepatitis C virus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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