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- PDB-3dfl: Crystal structure of human Prostasin complexed to 4-guanidinobenz... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3dfl | |||||||||
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Title | Crystal structure of human Prostasin complexed to 4-guanidinobenzoic acid | |||||||||
![]() | Prostasin | |||||||||
![]() | HYDROLASE / prostasin / serine protease / Glycoprotein / Membrane / Secreted / Transmembrane / Zymogen | |||||||||
Function / homology | ![]() Formation of the cornified envelope / positive regulation of sodium ion transport / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / serine-type peptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Su, H.P. / Rickert, K.W. / Darke, P.L. / Munshi, S.K. | |||||||||
![]() | ![]() Title: Structure of human prostasin, a target for the regulation of hypertension. Authors: Rickert, K.W. / Kelley, P. / Byrne, N.J. / Diehl, R.E. / Hall, D.L. / Montalvo, A.M. / Reid, J.C. / Shipman, J.M. / Thomas, B.W. / Munshi, S.K. / Darke, P.L. / Su, H.P. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 63.4 KB | Display | ![]() |
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PDB format | ![]() | 48.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.2 KB | Display | ![]() |
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Full document | ![]() | 436.5 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 20.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 28388.748 Da / Num. of mol.: 1 Fragment: Serine protease domain of prostasin heavy chain: Residues 45-289 Mutation: C154S, C203A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q16651, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases |
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#2: Chemical | ChemComp-GBS / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.84 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion / pH: 5.8 Details: 100mM Bis-Tris pH 5.8, 21-26% PEG 3350, VAPOR DIFFUSION, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Apr 15, 2008 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2→50 Å / Num. obs: 17151 / % possible obs: 99.8 % / Redundancy: 4.3 % / Rmerge(I) obs: 0.081 / Χ2: 1.019 / Net I/σ(I): 9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
Software |
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 51.86 Å2 / Biso mean: 18.038 Å2 / Biso min: 7.57 Å2
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Refinement step | Cycle: LAST / Resolution: 2→45.79 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.052 Å / Total num. of bins used: 20
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