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Yorodumi- PDB-2yp0: Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodies... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2yp0 | |||||||||
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Title | Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, crystallized with 2'-AMPS | |||||||||
Components | 2', 3'-CYCLIC NUCLEOTIDE 3'-PHOSPHODIESTERASE | |||||||||
Keywords | HYDROLASE / MYELIN / NERVOUS SYSTEM | |||||||||
Function / homology | Function and homology information cyclic nucleotide catabolic process / 2',3'-cyclic-nucleotide 3'-phosphodiesterase / 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity / myelin sheath abaxonal region / myelin sheath adaxonal region / cyclic nucleotide binding / regulation of mitochondrial membrane permeability / oligodendrocyte differentiation / pseudopodium / microvillus ...cyclic nucleotide catabolic process / 2',3'-cyclic-nucleotide 3'-phosphodiesterase / 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity / myelin sheath abaxonal region / myelin sheath adaxonal region / cyclic nucleotide binding / regulation of mitochondrial membrane permeability / oligodendrocyte differentiation / pseudopodium / microvillus / forebrain development / axonogenesis / adult locomotory behavior / cell projection / response to toxic substance / melanosome / myelin sheath / mitochondrial inner membrane / microtubule / mitochondrial outer membrane / response to lipopolysaccharide / perinuclear region of cytoplasm / extracellular space / RNA binding / membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | MUS MUSCULUS (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | |||||||||
Authors | Myllykoski, M. / Raasakka, A. / Lehtimaki, M. / Han, H. / Kursula, P. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 2013 Title: Crystallographic Analysis of the Reaction Cycle of 2',3'-Cyclic Nucleotide 3'-Phosphodiesterase, a Unique Member of the 2H Phosphoesterase Family Authors: Myllykoski, M. / Raasakka, A. / Lehtimaki, M. / Han, H. / Kursula, I. / Kursula, P. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2yp0.cif.gz | 136.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2yp0.ent.gz | 108.9 KB | Display | PDB format |
PDBx/mmJSON format | 2yp0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yp/2yp0 ftp://data.pdbj.org/pub/pdb/validation_reports/yp/2yp0 | HTTPS FTP |
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-Related structure data
Related structure data | 2yozC 2ypcC 2ypeC 2yphC 2yq9C 3zbrC 3zbsC 3zbzC 2xmiS S: Starting model for refinement 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
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 24293.928 Da / Num. of mol.: 1 / Fragment: C-TERMINAL CATALYTIC DOMAIN, RESIDUES 159-378 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA References: UniProt: P16330, 2',3'-cyclic-nucleotide 3'-phosphodiesterase |
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-Non-polymers , 5 types, 81 molecules
#2: Chemical | #3: Chemical | ChemComp-GOL / | #4: Chemical | ChemComp-1PE / | #5: Chemical | ChemComp-ACY / | #6: Water | ChemComp-HOH / | |
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-Details
Sequence details | N-TERMINAL GLYCINE REMAINS FROM TEV-CLEAVAGE OF EXPRESSION TAG. RESIDUE NUMBERING IS ACCORDING TO ...N-TERMINAL GLYCINE REMAINS FROM TEV-CLEAVAGE OF EXPRESSION |
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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: 1.9 Å3/Da / Density % sol: 36.6 % / Description: NONE |
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Crystal grow | pH: 4 Details: 250 UM PROTEIN AND 10 MM 2, 3(RP)-CYCLIC-AMPS MIXED WITH 0.5 PLUS 0.5 DROPS WITH 30% PEG4000 AND 50 MM ACETATE (MIX OF PH 3 AND PH 5 IN 2:1 RATIO) AT RT |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.815 |
Detector | Type: MAR555 FLAT PANEL / Detector: IMAGE PLATE / Date: Apr 3, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.815 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→19.4 Å / Num. obs: 8391 / % possible obs: 98.1 % / Observed criterion σ(I): -3 / Redundancy: 5.1 % / Biso Wilson estimate: 27.95 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 2.3→2.36 Å / Redundancy: 5.1 % / Rmerge(I) obs: 0.69 / Mean I/σ(I) obs: 2.5 / % possible all: 99.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2XMI Resolution: 2.3→19.29 Å / SU ML: 0.31 / σ(F): 1.99 / Phase error: 30.09 / Stereochemistry target values: ML Details: HYDROGENS WERE INCLUDED IN RIDING POSITIONS. RESIDUES 158-162 AND 208-213 WERE EXCLUDED DUE TO INSUFFICIENT ELECTRON DENSITY.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.93 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→19.29 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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