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Open data
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Basic information
Entry | Database: PDB / ID: 4br2 | ||||||
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Title | rat NTPDase2 in complex with Ca UMPPNP | ||||||
![]() | ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2 | ||||||
![]() | HYDROLASE / APYRASE / ATPASE / ADPASE / PURINERGIC SIGNALLING / DOMAIN ROTATION / TRANSITION STATE / NTPDASE | ||||||
Function / homology | ![]() purine ribonucleoside diphosphate catabolic process / Phosphate bond hydrolysis by NTPDase proteins / nucleoside diphosphate catabolic process / UDP phosphatase activity / nucleoside diphosphate phosphatase activity / ADP phosphatase activity / GDP 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 / UDP phosphatase activity / nucleoside diphosphate phosphatase activity / ADP phosphatase activity / GDP 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 / cellular response to tumor necrosis factor / cell body / 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 | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zebisch, M. / Schaefer, P. / Lauble, P. / Straeter, N. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 181.8 KB | Display | ![]() |
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PDB format | ![]() | 151.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 777 KB | Display | ![]() |
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Full document | ![]() | 781.9 KB | Display | |
Data in XML | ![]() | 21 KB | Display | |
Data in CIF | ![]() | 31 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4bqzC ![]() 4br0C ![]() 4br4C ![]() 4br5C ![]() 4br7C ![]() 4br9C ![]() 4braC ![]() 4brcC ![]() 4brdC ![]() 4breC ![]() 4brfC ![]() 4brgC ![]() 4brhC ![]() 4briC ![]() 4brkC ![]() 4brlC ![]() 4brmC ![]() 4brnC ![]() 4broC ![]() 4brpC ![]() 4brqC C: citing same article ( |
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Similar 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: 50699.027 Da / Num. of mol.: 1 / Fragment: ECTODOMAIN, RESIDUES 28-462 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: O35795, Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides, apyrase | ||||
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#2: Chemical | ChemComp-UNP / | ||||
#3: Chemical | ChemComp-CA / | ||||
#4: Chemical | ChemComp-GOL / #5: Water | ChemComp-HOH / | Nonpolymer details | PHOSPHOAMI | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % / Description: NONE |
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Crystal grow | pH: 7.5 / Details: 100 MM HEPES/NAOH PH 7.5, 2.5% PEG6000, 3MM NAN3 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL |
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→37 Å / Num. obs: 32508 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 14.3 |
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Processing
Software | Name: REFMAC / Version: 5.7.0029 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: ![]() 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.55 Å2
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Refinement step | Cycle: LAST / Resolution: 2→37.11 Å
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Refine LS restraints |
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