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Yorodumi- PDB-1wpl: Crystal structure of the inhibitory form of rat GTP cyclohydrolas... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1wpl | ||||||
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Title | Crystal structure of the inhibitory form of rat GTP cyclohydrolase I/GFRP complex | ||||||
Components | (GTP cyclohydrolase ...GTP cyclohydrolase I) x 2 | ||||||
Keywords | HYDROLASE/PROTEIN BINDING / ENZYME-REGULATORY PROTEIN COMPLEX / HYDROLASE-PROTEIN BINDING COMPLEX | ||||||
Function / homology | Function and homology information dihydrobiopterin metabolic process / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / GTP cyclohydrolase binding / pteridine-containing compound biosynthetic process / regulation of lung blood pressure / GTP cyclohydrolase I / GTP cyclohydrolase I activity / neuromuscular process controlling posture / negative regulation of biosynthetic process / GTP-dependent protein binding ...dihydrobiopterin metabolic process / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / GTP cyclohydrolase binding / pteridine-containing compound biosynthetic process / regulation of lung blood pressure / GTP cyclohydrolase I / GTP cyclohydrolase I activity / neuromuscular process controlling posture / negative regulation of biosynthetic process / GTP-dependent protein binding / regulation of removal of superoxide radicals / tetrahydrobiopterin biosynthetic process / regulation of nitric oxide biosynthetic process / enzyme inhibitor activity / mitogen-activated protein kinase binding / dopamine biosynthetic process / negative regulation of cardiac muscle cell apoptotic process / amino acid binding / response to pain / positive regulation of heart rate / response to type II interferon / negative regulation of cellular senescence / response to tumor necrosis factor / tetrahydrofolate biosynthetic process / positive regulation of telomere maintenance via telomerase / negative regulation of blood pressure / regulation of blood pressure / vasodilation / positive regulation of neuron apoptotic process / melanosome / cytoplasmic vesicle / nuclear membrane / protein-containing complex assembly / response to lipopolysaccharide / GTPase activity / dendrite / calcium ion binding / protein-containing complex binding / GTP binding / enzyme binding / protein homodimerization activity / protein-containing complex / mitochondrion / zinc ion binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Maita, N. / Hatakeyama, K. / Okada, K. / Hakoshima, T. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: Structural basis of biopterin-induced inhibition of GTP cyclohydrolase I by GFRP, its feedback regulatory protein Authors: Maita, N. / Hatakeyama, K. / Okada, K. / Hakoshima, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wpl.cif.gz | 558.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wpl.ent.gz | 458.1 KB | Display | PDB format |
PDBx/mmJSON format | 1wpl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wp/1wpl ftp://data.pdbj.org/pub/pdb/validation_reports/wp/1wpl | HTTPS FTP |
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-Related structure data
Related structure data | 1is7S 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
-GTP cyclohydrolase ... , 2 types, 20 molecules ABCDEFGHIJKLMNOPQRST
#1: Protein | Mass: 25819.672 Da / Num. of mol.: 10 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pET-15b / Production host: Escherichia coli (E. coli) / References: UniProt: P22288, GTP cyclohydrolase I #2: Protein | Mass: 9683.225 Da / Num. of mol.: 10 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pET-15b / Production host: Escherichia coli (E. coli) / References: UniProt: P70552 |
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-Non-polymers , 5 types, 270 molecules
#3: Chemical | ChemComp-ZN / #4: Chemical | ChemComp-HBI / #5: Chemical | ChemComp-3PO / #6: Chemical | ChemComp-NA / #7: 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: 2.46 Å3/Da / Density % sol: 50 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 2-propanol, ammonium sulfate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 283K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1.282 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 27, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.282 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→30 Å / Num. obs: 83700 / % possible obs: 100 % / Redundancy: 6.4 % / Biso Wilson estimate: 58.5 Å2 / Rmerge(I) obs: 0.107 / Rsym value: 0.089 / Net I/σ(I): 7.6 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.465 / Mean I/σ(I) obs: 1.9 / Num. unique all: 12175 / Rsym value: 0.386 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1IS7 Resolution: 2.8→15 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.8→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.9 Å
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