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Yorodumi- PDB-2qg4: Crystal structure of human UDP-glucose dehydrogenase product comp... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2qg4 | ||||||
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Title | Crystal structure of human UDP-glucose dehydrogenase product complex with UDP-glucuronate | ||||||
Components | UDP-glucose 6-dehydrogenase | ||||||
Keywords | OXIDOREDUCTASE / UDP-GLUCOSE 6-DEHYDROGENASE / HEXAMER / STRUCTURAL GENOMICS / Structural Genomics Consortium / SGC | ||||||
Function / homology | Function and homology information Formation of the active cofactor, UDP-glucuronate / chondroitin sulfate biosynthetic process / UDP-glucose 6-dehydrogenase / UDP-glucose 6-dehydrogenase activity / UDP-glucuronate biosynthetic process / heparan sulfate proteoglycan biosynthetic process / glycosaminoglycan biosynthetic process / gastrulation with mouth forming second / protein hexamerization / neuron development ...Formation of the active cofactor, UDP-glucuronate / chondroitin sulfate biosynthetic process / UDP-glucose 6-dehydrogenase / UDP-glucose 6-dehydrogenase activity / UDP-glucuronate biosynthetic process / heparan sulfate proteoglycan biosynthetic process / glycosaminoglycan biosynthetic process / gastrulation with mouth forming second / protein hexamerization / neuron development / NAD binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Kavanagh, K.L. / Guo, K. / Bunkoczi, G. / Savitsky, P. / Pilka, E. / Bhatia, C. / Niesen, F. / Smee, C. / Berridge, G. / von Delft, F. ...Kavanagh, K.L. / Guo, K. / Bunkoczi, G. / Savitsky, P. / Pilka, E. / Bhatia, C. / Niesen, F. / Smee, C. / Berridge, G. / von Delft, F. / Weigelt, J. / Arrowsmith, C.H. / Sundstrom, M. / Edwards, A. / Oppermann, U. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: Structure and mechanism of human UDP-glucose 6-dehydrogenase. Authors: Egger, S. / Chaikuad, A. / Kavanagh, K.L. / Oppermann, U. / Nidetzky, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qg4.cif.gz | 790.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qg4.ent.gz | 641.9 KB | Display | PDB format |
PDBx/mmJSON format | 2qg4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2qg4_validation.pdf.gz | 5.2 MB | Display | wwPDB validaton report |
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Full document | 2qg4_full_validation.pdf.gz | 5.2 MB | Display | |
Data in XML | 2qg4_validation.xml.gz | 150.4 KB | Display | |
Data in CIF | 2qg4_validation.cif.gz | 222.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qg/2qg4 ftp://data.pdbj.org/pub/pdb/validation_reports/qg/2qg4 | HTTPS FTP |
-Related structure data
Related structure data | 2q3eSC 3itkC 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Beg auth comp-ID: PHE / Beg label comp-ID: PHE / End auth comp-ID: VAL / End label comp-ID: VAL / Refine code: 5 / Auth seq-ID: 2 - 466 / Label seq-ID: 3 - 467
NCS ensembles :
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-Components
-Protein , 1 types, 8 molecules ABCDEFGH
#1: Protein | Mass: 52083.418 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UGDH / Plasmid: PBEN1-SGC / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O60701, UDP-glucose 6-dehydrogenase |
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-Non-polymers , 5 types, 3027 molecules
#2: Chemical | ChemComp-NAD / #3: Chemical | ChemComp-UGA / #4: Chemical | ChemComp-CL / #5: Chemical | ChemComp-EDO / #6: Water | ChemComp-HOH / | |
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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: 3.06 Å3/Da / Density % sol: 59.75 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 20% PEG 3350, 10% Ethylene glycol, 0.2 M NaBr, 0.1 M Bis-tris-propane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1.033 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 16, 2007 |
Radiation | Monochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.033 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→60 Å / Num. all: 288088 / Num. obs: 288088 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Biso Wilson estimate: 17 Å2 / Rmerge(I) obs: 0.139 / Net I/σ(I): 7.6 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 3.8 % / Mean I/σ(I) obs: 1.8 / Num. unique all: 42048 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 2Q3E Resolution: 2.1→59.66 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.939 / SU B: 8.234 / SU ML: 0.117 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.177 / ESU R Free: 0.165 / 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: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.44 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→59.66 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION
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