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Yorodumi- PDB-3wk2: Orotidine 5'-monophosphate decarboxylase K72A mutant from M. ther... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3wk2 | ||||||
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Title | Orotidine 5'-monophosphate decarboxylase K72A mutant from M. thermoautotrophicus complexed with orotidine 5'-monophosphate methyl ester | ||||||
Components | Orotidine 5'-phosphate decarboxylase | ||||||
Keywords | LYASE / protein-ligand complex / TIM barrel / decarboxylase / pyrimidine biosynthesis | ||||||
Function / homology | Function and homology information orotidine-5'-phosphate decarboxylase / orotidine-5'-phosphate decarboxylase activity / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | Methanothermobacter thermautotrophicus (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.69 Å | ||||||
Authors | Fujihashi, M. / Pai, E.F. / Miki, K. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2013 Title: Substrate distortion contributes to the catalysis of orotidine 5'-monophosphate decarboxylase. Authors: Fujihashi, M. / Ishida, T. / Kuroda, S. / Kotra, L.P. / Pai, E.F. / Miki, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3wk2.cif.gz | 113.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3wk2.ent.gz | 87.7 KB | Display | PDB format |
PDBx/mmJSON format | 3wk2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wk/3wk2 ftp://data.pdbj.org/pub/pdb/validation_reports/wk/3wk2 | HTTPS FTP |
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-Related structure data
Related structure data | 3wjwC 3wjxC 3wjyC 3wjzC 3wk0C 3wk1C 3wk3SC 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 on special symmetry positions |
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-Components
#1: Protein | Mass: 27321.299 Da / Num. of mol.: 1 / Mutation: K72A, L226R, N227I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanothermobacter thermautotrophicus (archaea) Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H Gene: pyrF, MTH_129 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) References: UniProt: O26232, orotidine-5'-phosphate decarboxylase | ||||
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#2: Chemical | ChemComp-O7M / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | ACCORDING TO DEPOSITORS, PRO101 IS CORRECT AND UNIPORT IS PROBABLY INCORRECT AT THIS POSITION. ...ACCORDING TO DEPOSITORS | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.63 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 8.5 Details: Sodium citrate, pH 8.5, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-ID-B / Wavelength: 1.0332 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD |
Radiation | Monochromator: Default / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 1.69→100 Å / Num. obs: 24736 / % possible obs: 99 % / Rmerge(I) obs: 0.052 / Net I/σ(I): 35.4 |
Reflection shell | Resolution: 1.69→1.73 Å / Rmerge(I) obs: 0.306 / Mean I/σ(I) obs: 6.1 / % possible all: 98.3 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 3WK3 Resolution: 1.69→51.71 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.955 / Occupancy max: 1 / Occupancy min: 0.3 / SU B: 3.497 / SU ML: 0.054 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.105 / ESU R Free: 0.094 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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 max: 71.56 Å2 / Biso mean: 17.1579 Å2 / Biso min: 5.91 Å2
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Refinement step | Cycle: LAST / Resolution: 1.69→51.71 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.69→1.734 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: 18.6859 Å / Origin y: 40.3505 Å / Origin z: 29.5694 Å
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Refinement TLS group |
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