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- PDB-1g0h: CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1g0h | ||||||
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Title | CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE-FRUCTOSE 1,6 BISPHOSPHATASE | ||||||
![]() | INOSITOL MONOPHOSPHATASE | ||||||
![]() | HYDROLASE / HOMODIMER / COMPLEXED WITH Ca2+ AND I-1-P | ||||||
Function / homology | ![]() inositol-phosphate phosphatase / inositol monophosphate 3-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 1-phosphatase activity / inositol metabolic process / fructose-bisphosphatase / fructose 1,6-bisphosphate 1-phosphatase activity / phosphatidylinositol phosphate biosynthetic process / signal transduction / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Johnson, K.A. / Chen, L. / Yang, H. / Roberts, M.F. / Stec, B. | ||||||
![]() | ![]() Title: Crystal structure and catalytic mechanism of the MJ0109 gene product: a bifunctional enzyme with inositol monophosphatase and fructose 1,6-bisphosphatase activities. Authors: Johnson, K.A. / Chen, L. / Yang, H. / Roberts, M.F. / Stec, B. #1: ![]() Title: MJ0109 is an Enzyme that is Both an Inositol Monophosphatse and the 'Missing' Archaeal Fructose-1,6-Bisphosphatase Authors: Stec, B. / Yang, H. / Johnson, K.A. / Chen, L. / Roberts, M.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 115.6 KB | Display | ![]() |
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PDB format | ![]() | 89.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 22.4 KB | Display | |
Data in CIF | ![]() | 30.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1g0iC ![]() 1awbS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Details | The biological assembly is a dimer constructed from chain A and B |
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Components
#1: Protein | Mass: 28611.838 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PET23A+ / Production host: ![]() ![]() #2: Chemical | ChemComp-CA / #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.81 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: PEG 8000, sodium chloride, calcium chloride, TRIS, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: UCSD MARK II / Detector: AREA DETECTOR / Date: Aug 27, 1997 |
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: 2.3→30 Å / Num. all: 29404 / Num. obs: 29087 / % possible obs: 97.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 46.1 Å2 / Rmerge(I) obs: 0.069 / Net I/σ(I): 12.2 |
Reflection shell | Resolution: 2.3→2.4 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.411 / Mean I/σ(I) obs: 1.1 / Num. unique all: 2879 / % possible all: 94.9 |
Reflection | *PLUS % possible obs: 98.7 % |
Reflection shell | *PLUS % possible obs: 95.9 % / Mean I/σ(I) obs: 1.2 |
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Processing
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Refinement | Starting model: 1AWB Resolution: 2.3→12 Å / Num. parameters: 16603 / Num. restraintsaints: 16745 / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber / Details: conjugated gradient least squares
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Solvent computation | Solvent model: MOEWS & KRETSINGER | |||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 0 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→12 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.221 / Rfactor obs: 0.174 / Rfactor Rfree: 0.235 / Rfactor Rwork: 0.174 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: s_angle_d / Dev ideal: 0.021 |