+Open data
-Basic information
Entry | Database: PDB / ID: 1ptk | ||||||
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Title | STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K | ||||||
Components | PROTEINASE K | ||||||
Keywords | HYDROLASE(SERINE PROTEINASE) | ||||||
Function / homology | Function and homology information peptidase K / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | Engyodontium album (fungus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Mueller, A. / Saenger, W. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1993 Title: Studies on the inhibitory action of mercury upon proteinase K. Authors: Muller, A. / Saenger, W. #1: Journal: Eur.J.Biochem. / Year: 1988 Title: Three-Dimensional Structure of Proteinase K at 0.15-Nm Resolution Authors: Betzel, C. / Pal, G.P. / Saenger, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ptk.cif.gz | 67.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ptk.ent.gz | 48.9 KB | Display | PDB format |
PDBx/mmJSON format | 1ptk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ptk_validation.pdf.gz | 420.4 KB | Display | wwPDB validaton report |
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Full document | 1ptk_full_validation.pdf.gz | 427 KB | Display | |
Data in XML | 1ptk_validation.xml.gz | 14.4 KB | Display | |
Data in CIF | 1ptk_validation.cif.gz | 21 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pt/1ptk ftp://data.pdbj.org/pub/pdb/validation_reports/pt/1ptk | HTTPS FTP |
-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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Atom site foot note | 1: CIS PROLINE - PRO 171 | ||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 28930.783 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Engyodontium album (fungus) / References: UniProt: P06873, peptidase K | ||||
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#2: Chemical | #3: Chemical | ChemComp-CA / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.79 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 8 Å / Num. obs: 8602 / % possible obs: 81 % / Observed criterion σ(F): 1 / Rmerge(I) obs: 0.041 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.4→8 Å / Rfactor obs: 0.126 / σ(F): 0 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→8 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 8 Å / σ(F): 0 / Rfactor all: 0.126 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 17.2 Å2 | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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