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- PDB-4ekf: Structure of the Inactive Adenovirus Proteinase at 0.98 Angstrom ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4ekf | ||||||
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Title | Structure of the Inactive Adenovirus Proteinase at 0.98 Angstrom Resolution | ||||||
![]() | Adenain | ||||||
![]() | HYDROLASE / alpha and beta protein (a+b) | ||||||
Function / homology | ![]() adenain / cysteine-type peptidase activity / virion component / cysteine-type endopeptidase activity / host cell nucleus / proteolysis / DNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Baniecki, M.L. / McGrath, W.J. / Mangel, W.F. | ||||||
![]() | ![]() Title: Regulation of a Viral Proteinase by a Peptide and DNA in One-dimensional Space: III. ATOMIC RESOLUTION STRUCTURE OF THE NASCENT FORM OF THE ADENOVIRUS PROTEINASE. Authors: Baniecki, M.L. / McGrath, W.J. / Mangel, W.F. #1: Journal: J.Biol.Chem. / Year: 2012 Title: Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. I. binding to DNA and to hexon of the precursor to protein VI, pVI, of human adenovirus. Authors: Graziano, V. / McGrath, W.J. / Suomalainen, M. / Greber, U.F. / Freimuth, P. / Blainey, P.C. / Luo, G. / Xie, X.S. / Mangel, W.F. #2: Journal: J.Biol.Chem. / Year: 2012 Title: Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. II. adenovirus proteinase is activated in an unusual one-dimensional biochemical reaction. Authors: Graziano, V. / Luo, G. / Blainey, P.C. / Perez-Berna, A.J. / McGrath, W.J. / Flint, S.J. / San Martin, C. / Xie, X.S. / Mangel, W.F. #3: Journal: J.Biol.Chem. / Year: 2012 Title: Regulation of a viral proteinase by a peptide and DNA in one-dimensional space. IV. viral proteinase slides along DNA to locate and process its substrates. Authors: Blainey, P.C. / Graziano, V. / Perez-Berna, A.J. / McGrath, W.J. / Flint, S.J. / San Martin, C. / Xie, X.S. / Mangel, W.F. #4: Journal: Acta Crystallogr.,Sect.D / Year: 2002 Title: Adenovirus proteinase: crystallization and preliminary X-ray diffraction studies to atomic resolution. Authors: Baniecki, M.L. / McGrath, W.J. / Dauter, Z. / Mangel, W.F. #5: ![]() Title: Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor. Authors: Ding, J. / McGrath, W.J. / Sweet, R.M. / Mangel, W.F. #6: ![]() Title: Crystallographic structure at 1.6-A resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: insights on a new fold. Authors: McGrath, W.J. / Ding, J. / Didwania, A. / Sweet, R.M. / Mangel, W.F. #7: Journal: Nature / Year: 1993 Title: Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity. Authors: Mangel, W.F. / McGrath, W.J. / Toledo, D.L. / Anderson, C.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 133.5 KB | Display | ![]() |
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PDB format | ![]() | 103.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.3 KB | Display | ![]() |
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Full document | ![]() | 439.2 KB | Display | |
Data in XML | ![]() | 12.7 KB | Display | |
Data in CIF | ![]() | 19.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1nlnS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23146.348 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-NA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.75 Å3/Da / Density % sol: 29.2 % |
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Crystal grow | Temperature: 293 K / pH: 5.6 Details: 0.3M sodium citrate, pH 5.6, 0.8 M sodium acetate, 5 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: BRANDEIS 4K / Detector: CCD / Date: Jul 28, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 0.98→30 Å / Num. obs: 92231 / % possible obs: 99.1 % / Redundancy: 4.9 % / Biso Wilson estimate: 8.59 Å2 / Rmerge(I) obs: 0.057 / Net I/σ(I): 25.4 |
Reflection shell | Resolution: 0.98→1 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.594 / % possible all: 97.1 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1NLN CHAIN A Resolution: 0.98→20 Å / Num. parameters: 16135 / Num. restraintsaints: 19747 / Occupancy max: 1 / Occupancy min: 0 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?
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Displacement parameters | Biso mean: 17.7814 Å2 | ||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.127 Å / Num. disordered residues: 12 / Occupancy sum hydrogen: 1406 / Occupancy sum non hydrogen: 1732.98 | ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.98→20 Å
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Refine LS restraints |
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