+Open data
-Basic information
Entry | Database: PDB / ID: 1is8 | ||||||
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Title | Crystal structure of rat GTPCHI/GFRP stimulatory complex plus Zn | ||||||
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 ...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 / regulation of removal of superoxide radicals / GTP-dependent protein binding / tetrahydrobiopterin biosynthetic process / regulation of nitric oxide biosynthetic process / enzyme inhibitor activity / dopamine biosynthetic process / mitogen-activated protein kinase binding / negative regulation of cardiac muscle cell apoptotic process / response to pain / amino acid binding / 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 / protein-containing complex assembly / nuclear membrane / 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 / MAD / Resolution: 2.7 Å | ||||||
Authors | Maita, N. / Okada, K. / Hatakeyama, K. / Hakoshima, T. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2002 Title: Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP. Authors: Maita, N. / Okada, K. / Hatakeyama, 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 | 1is8.cif.gz | 555.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1is8.ent.gz | 456.8 KB | Display | PDB format |
PDBx/mmJSON format | 1is8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/is/1is8 ftp://data.pdbj.org/pub/pdb/validation_reports/is/1is8 | HTTPS FTP |
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-Related 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: pMALc / 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 , 4 types, 401 molecules
#3: Chemical | ChemComp-ZN / #4: Chemical | ChemComp-K / #5: Chemical | ChemComp-PHE / #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: 2.43 Å3/Da / Density % sol: 49.32 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: MPD, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / Details: Maita, N., (2001) Acta Crystallogr., D57, 1153. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 1.2818 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 28, 2001 |
Radiation | Monochromator: Si(111) DOUBLE-CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.2818 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. all: 93244 / Num. obs: 93244 / % possible obs: 99.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 7.4 % / Biso Wilson estimate: 57.2 Å2 / Rsym value: 0.095 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 7.4 % / Mean I/σ(I) obs: 2.6 / Num. unique all: 13544 / Rsym value: 0.286 / % possible all: 99.9 |
Reflection | *PLUS Lowest resolution: 30 Å / Num. measured all: 693751 / Rmerge(I) obs: 0.095 |
Reflection shell | *PLUS Lowest resolution: 2.84 Å / % possible obs: 99.9 % / Rmerge(I) obs: 0.286 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.7→15 Å / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.7→15 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 15 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.216 / Rfactor Rfree: 0.243 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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