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Yorodumi- PDB-2xe6: The complete reaction cycle of human phosphoglycerate kinase: The... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2xe6 | ||||||
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Title | The complete reaction cycle of human phosphoglycerate kinase: The open binary complex with 3PG | ||||||
Components | PHOSPHOGLYCERATE KINASE 1 | ||||||
Keywords | TRANSFERASE / TRANSITION STATE ANALOGUE / HEREDITARY HEMOLYTIC ANEMIA / PHOSPHOPROTEIN / GLYCOLYSIS / PHOSPHORYL TRANSFER / NUCLEOTIDE-BINDING / DOMAIN MOTIONS | ||||||
Function / homology | Function and homology information Manipulation of host energy metabolism / phosphoglycerate kinase / phosphoglycerate kinase activity / protein-disulfide reductase (NAD(P)H) activity / Gluconeogenesis / canonical glycolysis / Glycolysis / plasminogen activation / epithelial cell differentiation / negative regulation of angiogenesis ...Manipulation of host energy metabolism / phosphoglycerate kinase / phosphoglycerate kinase activity / protein-disulfide reductase (NAD(P)H) activity / Gluconeogenesis / canonical glycolysis / Glycolysis / plasminogen activation / epithelial cell differentiation / negative regulation of angiogenesis / ADP binding / gluconeogenesis / glycolytic process / cellular response to hypoxia / membrane raft / phosphorylation / extracellular space / extracellular exosome / ATP binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.74 Å | ||||||
Authors | Cliff, M.J. / Baxter, N.J. / Blackburn, G.M. / Merli, A. / Vas, M. / Waltho, J.P. / Bowler, M.W. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: A Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase. Authors: Zerrad, L. / Merli, A. / Schroder, G.F. / Varga, A. / Graczer, E. / Pernot, P. / Round, A. / Vas, M. / Bowler, M.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2xe6.cif.gz | 172.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2xe6.ent.gz | 136.7 KB | Display | PDB format |
PDBx/mmJSON format | 2xe6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xe/2xe6 ftp://data.pdbj.org/pub/pdb/validation_reports/xe/2xe6 | HTTPS FTP |
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-Related structure data
Related structure data | 2xe7C 2xe8C 3c39S C: citing same article (ref.) S: Starting model for refinement |
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Similar 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: 44672.621 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET22A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P00558, phosphoglycerate kinase |
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#2: Chemical | ChemComp-3PG / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.3 % / Description: NONE |
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Crystal grow | pH: 8 / Details: 30% PEG4000, 100MM TRIS PH 8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jun 26, 2009 / Details: GE 221 |
Radiation | Monochromator: DIAMOND 110 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.74→20 Å / Num. obs: 43561 / % possible obs: 98.9 % / Observed criterion σ(I): 3 / Redundancy: 4.1 % / Biso Wilson estimate: 22.6 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 1.74→1.83 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.29 / Mean I/σ(I) obs: 3.2 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3C39 Resolution: 1.74→20 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.921 / SU B: 6.299 / SU ML: 0.091 / Cross valid method: THROUGHOUT / ESU R: 0.131 / ESU R Free: 0.131 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.249 Å2
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Refinement step | Cycle: LAST / Resolution: 1.74→20 Å
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Refine LS restraints |
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