[English] 日本語
Yorodumi- PDB-3e0n: The X-ray structure of Human Prostasin in complex with DFFR-chlor... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3e0n | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | The X-ray structure of Human Prostasin in complex with DFFR-chloromethyl ketone inhibitor | |||||||||
Components |
| |||||||||
Keywords | HYDROLASE / PROSTASIN / PROTEASE / chloromethyl-ketone / Channel / ENaC / Cell membrane / Glycoprotein / Membrane / Secreted / Serine protease / Transmembrane / Zymogen | |||||||||
Function / homology | Function and homology information 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 | Homo sapiens (human) synthetic construct (others) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | |||||||||
Authors | Spraggon, G. / Hornsby, M. / Shipway, A. / Harris, J.L. / Lesley, S.A. | |||||||||
Citation | Journal: Protein Sci. / Year: 2009 Title: Active site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cations. Authors: Spraggon, G. / Hornsby, M. / Shipway, A. / Tully, D.C. / Bursulaya, B. / Danahay, H. / Harris, J.L. / Lesley, S.A. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 3e0n.cif.gz | 117.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb3e0n.ent.gz | 87.6 KB | Display | PDB format |
PDBx/mmJSON format | 3e0n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e0/3e0n ftp://data.pdbj.org/pub/pdb/validation_reports/e0/3e0n | HTTPS FTP |
---|
-Related structure data
Related structure data | 3e1xC 3fvfC 3gylC 3gymC 1a0lS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 29608.002 Da / Num. of mol.: 1 / Fragment: UNP residues 45-305 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PRSS8 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q16651 | ||||
---|---|---|---|---|---|
#2: Protein/peptide | Type: Peptide-like / Class: Inhibitor / Mass: 466.576 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct / References: BIRD: PRD_002526 | ||||
#3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 1.91 Å3/Da / Density % sol: 35.65 % |
---|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.3 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 28, 2006 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 28770 / % possible obs: 98.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.5 % / Rmerge(I) obs: 0.096 / Rsym value: 0.096 / Net I/σ(I): 7.6 |
Reflection shell | Resolution: 1.7→1.79 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.491 / Mean I/σ(I) obs: 1.8 / Num. unique all: 3727 / Rsym value: 0.491 / % possible all: 89.9 |
-Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1A0L Resolution: 1.7→50 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.39 Å2
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→50 Å
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 1.7→1.7347 Å
|