+Open data
-Basic information
Entry | Database: PDB / ID: 5tnz | ||||||
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Title | HtrA2 S142D mutant | ||||||
Components | Serine protease HTRA2, mitochondrial | ||||||
Keywords | HYDROLASE / Mitochondrial protease / Serine protease / Trimeric Dynamics | ||||||
Function / homology | Function and homology information HtrA2 peptidase / pentacyclic triterpenoid metabolic process / negative regulation of mitophagy in response to mitochondrial depolarization / ceramide metabolic process / regulation of autophagy of mitochondrion / mitochondrial protein catabolic process / CD40 receptor complex / programmed cell death / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / protein serine/threonine kinase inhibitor activity ...HtrA2 peptidase / pentacyclic triterpenoid metabolic process / negative regulation of mitophagy in response to mitochondrial depolarization / ceramide metabolic process / regulation of autophagy of mitochondrion / mitochondrial protein catabolic process / CD40 receptor complex / programmed cell death / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / protein serine/threonine kinase inhibitor activity / serine-type endopeptidase complex / adult walking behavior / response to herbicide / positive regulation of protein targeting to mitochondrion / execution phase of apoptosis / positive regulation of execution phase of apoptosis / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / ubiquitin ligase inhibitor activity / protein autoprocessing / negative regulation of cell cycle / regulation of multicellular organism growth / cellular response to interferon-beta / neuron development / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / cellular response to retinoic acid / forebrain development / serine-type peptidase activity / mitochondrion organization / Mitochondrial protein degradation / protein catabolic process / mitochondrial membrane / mitochondrial intermembrane space / cytoplasmic side of plasma membrane / cellular response to growth factor stimulus / intrinsic apoptotic signaling pathway in response to DNA damage / unfolded protein binding / peptidase activity / cellular response to oxidative stress / cellular response to heat / neuron apoptotic process / negative regulation of neuron apoptotic process / cytoskeleton / intracellular signal transduction / positive regulation of apoptotic process / serine-type endopeptidase activity / endoplasmic reticulum membrane / chromatin / endoplasmic reticulum / mitochondrion / proteolysis / identical protein binding / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | ||||||
Authors | Macedo-Ribeiro, S. / Merski, M. / Pereira, P.J.B. | ||||||
Funding support | Portugal, 1items
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Citation | Journal: Cell Death Dis / Year: 2017 Title: Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2. Authors: Merski, M. / Moreira, C. / Abreu, R.M. / Ramos, M.J. / Fernandes, P.A. / Martins, L.M. / Pereira, P.J.B. / Macedo-Ribeiro, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5tnz.cif.gz | 131.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5tnz.ent.gz | 101.5 KB | Display | PDB format |
PDBx/mmJSON format | 5tnz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5tnz_validation.pdf.gz | 439.9 KB | Display | wwPDB validaton report |
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Full document | 5tnz_full_validation.pdf.gz | 442.6 KB | Display | |
Data in XML | 5tnz_validation.xml.gz | 14.1 KB | Display | |
Data in CIF | 5tnz_validation.cif.gz | 20 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tn/5tnz ftp://data.pdbj.org/pub/pdb/validation_reports/tn/5tnz | HTTPS FTP |
-Related structure data
Related structure data | 5m3nC 5m3oC 5tnyC 5to0C 5to1C 1lcyS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 36005.898 Da / Num. of mol.: 1 / Fragment: UNP residues 134-458 / Mutation: S142D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HTRA2, OMI, PRSS25 / Production host: Escherichia coli (E. coli) / References: UniProt: O43464, HtrA2 peptidase |
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#2: Chemical | ChemComp-MES / |
#3: Chemical | ChemComp-NA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.9 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 0.1 M MES pH 6.0, 1 M LiCl, and 15-20% (w/v) PEG-6000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.931 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 30, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→63 Å / Num. obs: 33463 / % possible obs: 100 % / Redundancy: 9.1 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 26.6 |
Reflection shell | Resolution: 1.75→1.84 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.369 / Mean I/σ(I) obs: 4.4 / Num. unique all: 4919 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1LCY Resolution: 1.75→62.945 Å / Cross valid method: FREE R-VALUE / σ(F): 2 / Phase error: 22.5
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→62.945 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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