+Open data
-Basic information
Entry | Database: PDB / ID: 1kc7 | ||||||
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Title | Pyruvate Phosphate Dikinase with Bound Mg-phosphonopyruvate | ||||||
Components | pyruvate phosphate dikinase | ||||||
Keywords | TRANSFERASE / PHOSPHOTRANSFERASE / KINASE / phosphonopyruvate inhibitor | ||||||
Function / homology | Function and homology information pyruvate, phosphate dikinase / pyruvate, phosphate dikinase activity / pyruvate metabolic process / kinase activity / phosphorylation / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | Clostridium symbiosum (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.2 Å | ||||||
Authors | Chen, C.C. / Howard, A. / Herzberg, O. | ||||||
Citation | Journal: Biochemistry / Year: 2002 Title: Pyruvate site of pyruvate phosphate dikinase: crystal structure of the enzyme-phosphonopyruvate complex, and mutant analysis Authors: Herzberg, O. / Chen, C.C. / Liu, S. / Tempczyk, A. / Howard, A. / Wei, M. / Ye, D. / Dunaway-Mariano, D. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1996 Title: SWIVELING-DOMAIN MECHANISM FOR ENZYMATIC PHOSPHOTRANSFER BETWEEN REMOTE REACTION SITES Authors: Herzberg, O. / Chen, C.C.H. / Kapadia, G. / Mcguire, M. / Carroll, L.J. / Noh, S.J. / Dunaway-Mariano, D. #2: Journal: Biochemistry / Year: 1998 Title: Location of the Phosphate Binding Site within Clostridium Symbiosum Pyruvate Phosphate dikinase Authors: Mcguire, M. / Huang, K. / Kapadia, G. / Herzberg, O. / Dunaway-Mariano, D. #3: Journal: J.Biol.Chem. / Year: 2000 Title: Identification of Domain-Domain Docking Sites within Clostridium Symbiosum Pyruvate Phosphate Dikinase by Amino Acid Replacement Authors: Wei, M. / Li, Z. / Ye, D. / Herzberg, O. / Dunaway-Mariano, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kc7.cif.gz | 180.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kc7.ent.gz | 141.5 KB | Display | PDB format |
PDBx/mmJSON format | 1kc7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1kc7_validation.pdf.gz | 438 KB | Display | wwPDB validaton report |
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Full document | 1kc7_full_validation.pdf.gz | 463.5 KB | Display | |
Data in XML | 1kc7_validation.xml.gz | 22.7 KB | Display | |
Data in CIF | 1kc7_validation.cif.gz | 32.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kc/1kc7 ftp://data.pdbj.org/pub/pdb/validation_reports/kc/1kc7 | HTTPS FTP |
-Related structure data
Related structure data | 1kblC 1dikS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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Details | A dimer generated by a crystallographic 2-fold axis: -1.0 0.0 0.0 89.837 0.0 1.0 0.0 0.0 0.0 0.0 -1.0 0.0 |
-Components
#1: Protein | Mass: 96640.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium symbiosum (bacteria) / Gene: PPDK / Plasmid: PACYC184-D12 / Production host: Escherichia coli (E. coli) / Strain (production host): JM 101 / References: UniProt: P22983, pyruvate, phosphate dikinase | ||
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#2: Chemical | ChemComp-MG / | ||
#3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-PPR / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.33 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 303 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 54% saturated ammonium sulfate, 100mM Hepes buffer (pH 7.0), 9mg/ml protein solution consisting of: 20mM imidazole buffer (pH 6.5), 100mM KCl, 40mM phosphonopyruvate, 5mM MgCl2, 0.1mM EDTA, ...Details: 54% saturated ammonium sulfate, 100mM Hepes buffer (pH 7.0), 9mg/ml protein solution consisting of: 20mM imidazole buffer (pH 6.5), 100mM KCl, 40mM phosphonopyruvate, 5mM MgCl2, 0.1mM EDTA, 1mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 303K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 30 ℃ / pH: 6.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: APS / Beamline: 17-ID / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 6, 2001 / Details: mirror |
Radiation | Monochromator: CRYOGENITCALLY-COOLED SI(111) DOUBLE CRYSTAL system Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.73→25 Å / Num. all: 104444 / Num. obs: 104444 / % possible obs: 95.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Biso Wilson estimate: 40.8 Å2 / Rmerge(I) obs: 0.114 / Net I/σ(I): 26.6 |
Reflection shell | Resolution: 1.73→1.79 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 4.1 / Num. unique all: 14814 / % possible all: 81.4 |
Reflection | *PLUS |
Reflection shell | *PLUS % possible obs: 81.4 % / Num. unique obs: 14814 / Rmerge(I) obs: 0.523 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 1DIK Resolution: 2.2→25 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.2→25 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 25 Å / Num. reflection obs: 49319 / σ(F): 2 / % reflection Rfree: 4.8 % / Rfactor obs: 0.198 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: c_angle_deg / Dev ideal: 1.9 |