+Open data
-Basic information
Entry | Database: PDB / ID: 4bpv | ||||||
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Title | MOUSE CATHEPSIN S WITH COVALENT LIGAND | ||||||
Components | CATHEPSIN S | ||||||
Keywords | HYDROLASE / CYSTEINE PROTEASE / COVALENT LIGAND | ||||||
Function / homology | Function and homology information Assembly of collagen fibrils and other multimeric structures / Trafficking and processing of endosomal TLR / cathepsin S / basement membrane disassembly / Degradation of the extracellular matrix / positive regulation of cation channel activity / MHC class II antigen presentation / cysteine-type endopeptidase activator activity involved in apoptotic process / bone resorption / phagocytic vesicle ...Assembly of collagen fibrils and other multimeric structures / Trafficking and processing of endosomal TLR / cathepsin S / basement membrane disassembly / Degradation of the extracellular matrix / positive regulation of cation channel activity / MHC class II antigen presentation / cysteine-type endopeptidase activator activity involved in apoptotic process / bone resorption / phagocytic vesicle / cysteine-type peptidase activity / Neutrophil degranulation / early endosome lumen / proteolysis involved in protein catabolic process / positive regulation of apoptotic signaling pathway / positive regulation of inflammatory response / antigen processing and presentation of exogenous peptide antigen via MHC class II / peptidase activity / lysosome / immune response / cysteine-type endopeptidase activity / cell surface / proteolysis / extracellular space / membrane Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Banner, D.W. / Benz, J. / Gsell, B. / Stihle, M. / Ruf, A. / Haap, W. | ||||||
Citation | Journal: To be Published Title: Cathepsin S Nitrile Inhibitors Authors: Haap, W. / Banner, D.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4bpv.cif.gz | 260.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4bpv.ent.gz | 211.2 KB | Display | PDB format |
PDBx/mmJSON format | 4bpv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4bpv_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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Full document | 4bpv_full_validation.pdf.gz | 2 MB | Display | |
Data in XML | 4bpv_validation.xml.gz | 57.6 KB | Display | |
Data in CIF | 4bpv_validation.cif.gz | 79.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bp/4bpv ftp://data.pdbj.org/pub/pdb/validation_reports/bp/4bpv | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 24662.480 Da / Num. of mol.: 6 / Fragment: RESIDUES 116-340 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: O70370, cathepsin S #2: Chemical | ChemComp-OFH / ( #3: Water | ChemComp-HOH / | Has protein modification | Y | Sequence details | 116-340 NO MUTATIONS | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.45 Å3/Da / Density % sol: 64.4 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: 25% PEG 3350, 0.1 M HEPES PH7.5, 0.2M NH4AC |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Aug 12, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→45.1 Å / Num. obs: 128672 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 3.78 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 10.33 |
Reflection shell | Resolution: 1.95→2 Å / Redundancy: 3.52 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 1.84 / % possible all: 97.3 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: IN HOUSE STRUCTURES Resolution: 2→45.11 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.906 / SU B: 4.487 / SU ML: 0.123 / Cross valid method: THROUGHOUT / ESU R: 0.167 / ESU R Free: 0.159 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS BUT NOT OUTPUT. U VALUES REFINED INDIVIDUALLY. CHAINS A,B,C,D FORM LAYERS. E BRIDGES THE LAYERS AND K IS ONLY PARTIALLY VISIBLE
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.644 Å2
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Refinement step | Cycle: LAST / Resolution: 2→45.11 Å
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Refine LS restraints |
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