+Open data
-Basic information
Entry | Database: PDB / ID: 1vzv | ||||||
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Title | STRUCTURE OF VARICELLA-ZOSTER VIRUS PROTEASE | ||||||
Components | VARICELLA-ZOSTER VIRUS PROTEASE | ||||||
Keywords | SERINE PROTEASE / HYDROLASE / VIRAL PROTEASE / VARICELLA-ZOSTER VIRUS / COAT PROTEIN | ||||||
Function / homology | Function and homology information nuclear capsid assembly / assemblin / viral release from host cell / host cell cytoplasm / serine-type endopeptidase activity / host cell nucleus / identical protein binding Similarity search - Function | ||||||
Biological species | Human herpesvirus 3 (Varicella-zoster virus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Qiu, X. / Jason, C.A. / Culp, J.S. / Richardson, S.B. / Debouck, C. / Smith, W.W. / Abdel-Meguid, S.S. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1997 Title: Crystal structure of varicella-zoster virus protease. Authors: Qiu, X. / Janson, C.A. / Culp, J.S. / Richardson, S.B. / Debouck, C. / Smith, W.W. / Abdel-Meguid, S.S. #1: Journal: Nature / Year: 1996 Title: Unique Fold and Active Site in Cytomegalovirus Protease Authors: Qiu, X. / Culp, J.S. / Dilella, A.G. / Hellmig, B. / Hoog, S.S. / Janson, C.A. / Smith, W.W. / Abdel-Meguid, S.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vzv.cif.gz | 47 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vzv.ent.gz | 32.9 KB | Display | PDB format |
PDBx/mmJSON format | 1vzv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vz/1vzv ftp://data.pdbj.org/pub/pdb/validation_reports/vz/1vzv | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 24654.525 Da / Num. of mol.: 1 / Fragment: RESIDUES 10 - 236 / Mutation: C10M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 3 (Varicella-zoster virus) Genus: Varicellovirus / Strain: ACYCLOVIR-RESISTANT STRAIN 40A2 / Production host: Escherichia coli (E. coli) References: UniProt: P09286, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 60 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Dec 28, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 5419 / % possible obs: 90 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.07 |
Reflection | *PLUS Highest resolution: 3 Å |
-Processing
Software |
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Refinement | Resolution: 3→7 Å / σ(F): 2 /
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Displacement parameters | Biso mean: 25 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3→7 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 25 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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