+Open data
-Basic information
Entry | Database: PDB / ID: 4br0 | ||||||
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Title | rat NTPDase2 in complex with Ca AMPNP | ||||||
Components | ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2 | ||||||
Keywords | HYDROLASE / APYRASE / ATPASE / ADPASE / PURINERGIC SIGNALLING / DOMAIN ROTATION / TRANSITION STATE / NTPDASE | ||||||
Function / homology | Function and homology information purine ribonucleoside diphosphate catabolic process / Phosphate bond hydrolysis by NTPDase proteins / nucleoside diphosphate catabolic process / nucleoside diphosphate phosphatase activity / UDP phosphatase activity / GDP phosphatase activity / ADP phosphatase activity / cellular response to interferon-alpha / response to auditory stimulus / cell projection membrane ...purine ribonucleoside diphosphate catabolic process / Phosphate bond hydrolysis by NTPDase proteins / nucleoside diphosphate catabolic process / nucleoside diphosphate phosphatase activity / UDP phosphatase activity / GDP phosphatase activity / ADP phosphatase activity / cellular response to interferon-alpha / response to auditory stimulus / cell projection membrane / cellular response to interleukin-6 / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / basement membrane / ribonucleoside triphosphate phosphatase activity / platelet activation / cell body / cellular response to tumor necrosis factor / cellular response to lipopolysaccharide / G protein-coupled receptor signaling pathway / cell surface / ATP hydrolysis activity / ATP binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | RATTUS NORVEGICUS (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 2.05 Å | ||||||
Authors | Zebisch, M. / Schaefer, P. / Lauble, P. / Straeter, N. | ||||||
Citation | Journal: Structure / Year: 2013 Title: Crystallographic Snapshots Along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases Authors: Zebisch, M. / Krauss, M. / Schaefer, P. / Lauble, P. / Straeter, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4br0.cif.gz | 178.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4br0.ent.gz | 148.8 KB | Display | PDB format |
PDBx/mmJSON format | 4br0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/br/4br0 ftp://data.pdbj.org/pub/pdb/validation_reports/br/4br0 | HTTPS FTP |
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-Related structure data
Related structure data | 4bqzC 4br2C 4br4C 4br5C 4br7C 4br9C 4braC 4brcC 4brdC 4breC 4brfC 4brgC 4brhC 4briC 4brkC 4brlC 4brmC 4brnC 4broC 4brpC 4brqC C: citing same article (ref.) |
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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: 50699.027 Da / Num. of mol.: 1 / Fragment: RESIDUES 28-462 Source method: isolated from a genetically manipulated source Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Production host: ESCHERICHIA COLI (E. coli) References: UniProt: O35795, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides, apyrase | ||||
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#2: Chemical | ChemComp-AU1 / | ||||
#3: Chemical | ChemComp-CA / | ||||
#4: Chemical | ChemComp-GOL / #5: Water | ChemComp-HOH / | Nonpolymer details | (3S)-3-HYDROXY-1-METHYL-2,3-DIHYDRO-1H-INDOLE-5,6-DIONE (AU1): AMPNP ADP ANALOG | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % / Description: NONE |
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Crystal grow | Details: 100 MM HEPES/NAOH PH 7.3, 2% PEG6000, 3MM NAN3 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9184 |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→36.7 Å / Num. obs: 30057 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 6.3 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 16 |
-Processing
Software | Name: REFMAC / Version: 5.7.0029 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 2.05→19.71 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.947 / SU B: 6.92 / SU ML: 0.099 / Cross valid method: THROUGHOUT / ESU R: 0.171 / ESU R Free: 0.158 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES WITH TLS ADDED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.044 Å2
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Refinement step | Cycle: LAST / Resolution: 2.05→19.71 Å
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