+Open data
-Basic information
Entry | Database: PDB / ID: 1dbz | ||||||
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Title | C153S MUTANT OF PEA FRUCTOSE-1,6-BISPHOSPHATASE | ||||||
Components | FRUCTOSE-1,6-BISPHOSPHATASEFructose 1,6-bisphosphatase | ||||||
Keywords | HYDROLASE / CHLOROPLAST / PHOTOSYNTHESIS / REDOX REGULATION / THIOREDOXIN / ALLOSTERY / DISULFIDE BRIDGE / CALVIN CYCLE | ||||||
Function / homology | Function and homology information reductive pentose-phosphate cycle / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / chloroplast stroma / metal ion binding Similarity search - Function | ||||||
Biological species | Pisum sativum (garden pea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å | ||||||
Authors | Chiadmi, M. / Navaza, A. / Miginiac-Maslow, M. / Jacquot, J.P. / Cherfils, J. | ||||||
Citation | Journal: EMBO J. / Year: 1999 Title: Redox signalling in the chloroplast: structure of oxidized pea fructose-1,6-bisphosphate phosphatase. Authors: Chiadmi, M. / Navaza, A. / Miginiac-Maslow, M. / Jacquot, J.P. / Cherfils, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dbz.cif.gz | 242.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dbz.ent.gz | 197 KB | Display | PDB format |
PDBx/mmJSON format | 1dbz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/db/1dbz ftp://data.pdbj.org/pub/pdb/validation_reports/db/1dbz | 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
#1: Protein | Mass: 39225.961 Da / Num. of mol.: 4 / Mutation: C153S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pisum sativum (garden pea) / Organelle: CHLOROPLAST / Production host: Escherichia coli (E. coli) / References: UniProt: P46275, fructose-bisphosphatase |
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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: 2.47 Å3/Da / Density % sol: 50.3 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 20% PEG 1000, 50MM NA ACETATE (PH 5), 50 MM MGCL2, 5MM F6P, VAPOR DIFFUSION, HANGING DROP, temperature 291K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SYNCHROTRON / Site: LURE / Beamline: D41A / Wavelength: 1.375 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.375 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→18 Å / Num. all: 43470 / Num. obs: 41334 / % possible obs: 87.6 % / Redundancy: 7 % / Biso Wilson estimate: 60 Å2 / Rmerge(I) obs: 0.096 / Net I/σ(I): 13 |
Reflection shell | Resolution: 2.65→2.7 Å / Redundancy: 4 % / Rmerge(I) obs: 0.9 / Num. unique all: 2000 / % possible all: 89 |
Reflection | *PLUS Num. measured all: 291800 |
Reflection shell | *PLUS % possible obs: 89 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: OXIDIZED PEA WILD TYPE FBPASE FORM 1 Resolution: 2.65→10 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.65→10 Å
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Refine LS restraints |
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