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Yorodumi- PDB-1jg5: CRYSTAL STRUCTURE OF RAT GTP CYCLOHYDROLASE I FEEDBACK REGULATORY... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jg5 | ||||||
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Title | CRYSTAL STRUCTURE OF RAT GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN, GFRP | ||||||
Components | GTP CYCLOHYDROLASE I FEEDBACK REGULATORY PROTEIN | ||||||
Keywords | PROTEIN BINDING / alpha/beta structure / beta sheet | ||||||
Function / homology | Function and homology information Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / GTP cyclohydrolase binding / negative regulation of biosynthetic process / GTP-dependent protein binding / regulation of nitric oxide biosynthetic process / enzyme inhibitor activity / amino acid binding / melanosome / protein-containing complex assembly / nuclear membrane ...Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / GTP cyclohydrolase binding / negative regulation of biosynthetic process / GTP-dependent protein binding / regulation of nitric oxide biosynthetic process / enzyme inhibitor activity / amino acid binding / melanosome / protein-containing complex assembly / nuclear membrane / dendrite / protein-containing complex binding / enzyme binding / protein-containing complex / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.6 Å | ||||||
Authors | Bader, G. / Schiffmann, S. / Herrmann, A. / Fischer, M. / Gutlich, M. / Auerbach, G. / Ploom, T. / Bacher, A. / Huber, R. / Lemm, T. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2001 Title: Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP. Authors: Bader, G. / Schiffmann, S. / Herrmann, A. / Fischer, M. / Gutlich, M. / Auerbach, G. / Ploom, T. / Bacher, A. / Huber, R. / Lemm, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jg5.cif.gz | 98.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jg5.ent.gz | 76.5 KB | Display | PDB format |
PDBx/mmJSON format | 1jg5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jg5_validation.pdf.gz | 446 KB | Display | wwPDB validaton report |
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Full document | 1jg5_full_validation.pdf.gz | 450.4 KB | Display | |
Data in XML | 1jg5_validation.xml.gz | 20.2 KB | Display | |
Data in CIF | 1jg5_validation.cif.gz | 28.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jg/1jg5 ftp://data.pdbj.org/pub/pdb/validation_reports/jg/1jg5 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 9552.030 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: PQE(7) / Production host: Escherichia coli (E. coli) / Strain (production host): XL1 / References: UniProt: P70552 #2: Chemical | ChemComp-K / #3: 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: 2.38 Å3/Da / Density % sol: 48.3 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: batch crystallization / pH: 7.4 Details: 100mM potassium phosphate, 2mM DTT, pH 7.4, batch crystallization, temperature 293K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: batch method | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Details: mirrors |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→35 Å / Num. obs: 14791 / % possible obs: 97.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.118 |
Reflection shell | Resolution: 2.6→2.65 Å |
Reflection | *PLUS Lowest resolution: 35 Å / Num. measured all: 154398 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.6→30 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.6→30 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 30 Å / σ(F): 2 / Rfactor obs: 0.166 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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