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Yorodumi- PDB-6hfq: Human dihydroorotase mutant F1563T co-crystallized with carbamoyl... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6hfq | ||||||
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Title | Human dihydroorotase mutant F1563T co-crystallized with carbamoyl aspartate at pH 7.5 | ||||||
Components | CAD protein | ||||||
Keywords | BIOSYNTHETIC PROTEIN / de novo pyrimidine biosynthesis / CAD / TIM-barrel / carboxylated lysine | ||||||
Function / homology | Function and homology information aspartate binding / response to cortisol / carbamoyl-phosphate synthase (glutamine-hydrolysing) / carbamoyl-phosphate synthase (ammonia) / carbamoyl-phosphate synthase (ammonia) activity / carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity / dihydroorotase / citrulline biosynthetic process / aspartate carbamoyltransferase / glutaminase ...aspartate binding / response to cortisol / carbamoyl-phosphate synthase (glutamine-hydrolysing) / carbamoyl-phosphate synthase (ammonia) / carbamoyl-phosphate synthase (ammonia) activity / carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity / dihydroorotase / citrulline biosynthetic process / aspartate carbamoyltransferase / glutaminase / aspartate carbamoyltransferase activity / dihydroorotase activity / Pyrimidine biosynthesis / glutaminase activity / UDP biosynthetic process / UTP biosynthetic process / response to caffeine / response to testosterone / glutamine metabolic process / response to starvation / response to amine / cellular response to epidermal growth factor stimulus / 'de novo' UMP biosynthetic process / animal organ regeneration / 'de novo' pyrimidine nucleobase biosynthetic process / lactation / xenobiotic metabolic process / liver development / cell projection / female pregnancy / peptidyl-threonine phosphorylation / response to insulin / terminal bouton / nuclear matrix / heart development / protein autophosphorylation / protein kinase activity / neuronal cell body / enzyme binding / protein-containing complex / zinc ion binding / extracellular exosome / ATP binding / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.14542458871 Å | ||||||
Authors | Ramon-Maiques, S. / Grande Garcia, A. | ||||||
Funding support | Spain, 1items
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Citation | Journal: J. Biol. Chem. / Year: 2018 Title: Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD. Authors: Del Cano-Ochoa, F. / Grande-Garcia, A. / Reverte-Lopez, M. / D'Abramo, M. / Ramon-Maiques, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6hfq.cif.gz | 287.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6hfq.ent.gz | 193.2 KB | Display | PDB format |
PDBx/mmJSON format | 6hfq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6hfq_validation.pdf.gz | 475.6 KB | Display | wwPDB validaton report |
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Full document | 6hfq_full_validation.pdf.gz | 476.2 KB | Display | |
Data in XML | 6hfq_validation.xml.gz | 18.6 KB | Display | |
Data in CIF | 6hfq_validation.cif.gz | 28.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hf/6hfq ftp://data.pdbj.org/pub/pdb/validation_reports/hf/6hfq | HTTPS FTP |
-Related structure data
Related structure data | 6hfdC 6hfeC 6hffC 6hfhC 6hfiC 6hfjC 6hfkC 6hflC 6hfnC 6hfpC 6hfrC 6hfsC 6hfuC 6hg1C 6hg2C 6hg3C 4c6iS 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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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 42855.922 Da / Num. of mol.: 1 / Mutation: F1563T Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CAD / Plasmid: pOPIN-M / Cell line (production host): HEK293 GnTI / Production host: Homo sapiens (human) References: UniProt: P27708, carbamoyl-phosphate synthase (glutamine-hydrolysing), aspartate carbamoyltransferase, dihydroorotase |
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-Non-polymers , 5 types, 360 molecules
#2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-DOR / ( | #4: Chemical | ChemComp-FMT / #5: Chemical | ChemComp-GOL / | #6: Water | ChemComp-HOH / | |
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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: 2.52 Å3/Da / Density % sol: 51.11 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: Protein at 2-3 mg/ml in 20 mM Tris pH 8, 0.15 M NaCl, 0.02 mM zinc sulfate, 0.2 mM TCEP with 4 mM carbamoyl asparate. Mother liquor: 2.5-3 M potassium formate, 0.1 M HEPES pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 1 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 22, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.14541881133→35.9537720577 Å / Num. obs: 131901 / % possible obs: 92.4 % / Redundancy: 6.8 % / Biso Wilson estimate: 13.2364773568 Å2 / CC1/2: 0.999 / Rrim(I) all: 0.051 / Net I/σ(I): 20.8 |
Reflection shell | Resolution: 1.14541881133→1.19 Å / Redundancy: 5.8 % / Mean I/σ(I) obs: 3.4 / Num. unique obs: 10121 / CC1/2: 0.928 / Rrim(I) all: 0.511 / % possible all: 71.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4c6i Resolution: 1.14542458871→35.9537720577 Å / SU ML: 0.0560322366889 / Cross valid method: FREE R-VALUE / σ(F): 1.33652856263 / Phase error: 11.7444026315
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.7193285176 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.14542458871→35.9537720577 Å
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Refine LS restraints |
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LS refinement shell |
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