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- PDB-1lbv: Crystal Structure of apo-form (P21) of dual activity FBPase/IMPas... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lbv | ||||||
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Title | Crystal Structure of apo-form (P21) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus | ||||||
![]() | fructose 1,6-bisphosphatase/inositol monophosphatase | ||||||
![]() | HYDROLASE / dual activity / FBPase / IMPase / archaeal phosphatase / apo-form | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Stieglitz, K.A. / Johnson, K.A. / Yang, H. / Roberts, M.F. / Seaton, B.A. / Head, J.F. / Stec, B. | ||||||
![]() | ![]() Title: Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. Authors: Stieglitz, K.A. / Johnson, K.A. / Yang, H. / Roberts, M.F. / Seaton, B.A. / Head, J.F. / Stec, B. #1: ![]() 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. | ||||||
History |
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Remark 999 | SEQUENCE THIS SEQUENCE IS ANNOTATED IN THE PIR ENTRY D69546 AS SUHB ANALOGUE, WHICH WAS BASED ON ...SEQUENCE THIS SEQUENCE IS ANNOTATED IN THE PIR ENTRY D69546 AS SUHB ANALOGUE, WHICH WAS BASED ON SEQUENCE HOMOLOGIES, NOT BIOCHEMICAL ASSAYS. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 113.5 KB | Display | ![]() |
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PDB format | ![]() | 87.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.9 KB | Display | ![]() |
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Full document | ![]() | 451.1 KB | Display | |
Data in XML | ![]() | 23.2 KB | Display | |
Data in CIF | ![]() | 32.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1lbwC ![]() 1lbxC ![]() 1lbyC ![]() 1lbzC ![]() 1dk4S 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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Unit cell |
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Components
#1: Protein | Mass: 28002.838 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: O30298, fructose-bisphosphatase, inositol-phosphate phosphatase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.95 Å3/Da / Density % sol: 37.04 % | ||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG 3350, ammonium phosphate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 13, 2000 |
Radiation | Monochromator: collimating mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.009 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→40 Å / Num. all: 38204 / Num. obs: 37007 / % possible obs: 96.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 2.1 % / Rmerge(I) obs: 0.036 / Net I/σ(I): 16.8 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.274 / Mean I/σ(I) obs: 3.2 / Num. unique all: 3370 / % possible all: 86.2 |
Reflection | *PLUS Num. obs: 35243 / % possible obs: 93.7 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.036 |
Reflection shell | *PLUS % possible obs: 83.9 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.27 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1DK4 Resolution: 1.8→31.81 Å / Num. parameters: 16663 / Num. restraintsaints: 16078 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber / Details: SHELXL CONJUGATED GRADIENT
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Solvent computation | Solvent model: MOEWS & KRETSINGER | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→31.81 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS σ(F): 4 / % reflection Rfree: 4 % / Rfactor all: 0.215 / Rfactor obs: 0.203 / Rfactor Rfree: 0.273 / Rfactor Rwork: 0.203 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: s_bond_d / Dev ideal: 0.007 |