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Yorodumi- PDB-3itk: Crystal structure of human UDP-glucose dehydrogenase Thr131Ala, a... -
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-Basic information
Entry | Database: PDB / ID: 3itk | ||||||
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Title | Crystal structure of human UDP-glucose dehydrogenase Thr131Ala, apo form. | ||||||
Components | UDP-glucose 6-dehydrogenase | ||||||
Keywords | OXIDOREDUCTASE / Structural Genomics / Structural Genomics Consortium / SGC / NAD / Phosphoprotein | ||||||
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: 2.4 Å | ||||||
Authors | Chaikuad, A. / Egger, S. / Yue, W.W. / Sethi, R. / Filippakopoulos, P. / Muniz, J.R.C. / von Delft, F. / Bountra, C. / Arrowsmith, C.H. / Weigelt, J. ...Chaikuad, A. / Egger, S. / Yue, W.W. / Sethi, R. / Filippakopoulos, P. / Muniz, J.R.C. / von Delft, F. / Bountra, C. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Kavanagh, K.L. / Nidetzky, B. / 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 | 3itk.cif.gz | 559.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3itk.ent.gz | 460.7 KB | Display | PDB format |
PDBx/mmJSON format | 3itk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3itk_validation.pdf.gz | 493 KB | Display | wwPDB validaton report |
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Full document | 3itk_full_validation.pdf.gz | 513.7 KB | Display | |
Data in XML | 3itk_validation.xml.gz | 106.3 KB | Display | |
Data in CIF | 3itk_validation.cif.gz | 150.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/it/3itk ftp://data.pdbj.org/pub/pdb/validation_reports/it/3itk | HTTPS FTP |
-Related structure data
Related structure data | 2q3eSC 2qg4C 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 ensembles :
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Details | THE HEXAMER IN THE ASYMMETRIC UNIT REPRESENTS THE HEXAMERIC BIOLOGICAL UNIT. |
-Components
#1: Protein | Mass: 52053.395 Da / Num. of mol.: 6 / Fragment: UNP residues 1-466 / Mutation: T131A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: UGDH / Plasmid: pBEN1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-R3-pRARE2 / References: UniProt: O60701, UDP-glucose 6-dehydrogenase #2: Chemical | ChemComp-PG4 / #3: Chemical | ChemComp-EDO / #4: 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: 2.65 Å3/Da / Density % sol: 53.64 % |
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Crystal grow | Temperature: 293.15 K / pH: 6 Details: 15% PEG smears (PEG 400, 600, 1000, 2000, 3350, 4000, MME 5000, 6000, 8000, 10000), 0.1M MES pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 15, 2009 / Details: MIRRORS |
Radiation | Monochromator: SI(111) DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→52.9 Å / Num. obs: 130411 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Biso Wilson estimate: 40.1 Å2 / Rmerge(I) obs: 0.131 / Net I/σ(I): 7.9 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 2.1 / % possible all: 99.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2Q3E Resolution: 2.4→52.9 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.906 / SU B: 16.607 / SU ML: 0.174 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.381 / ESU R Free: 0.246 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES: RESIDUAL ONLY. THE NCS RESTRAINTS HAVE BEEN USED IN REFINEMENT.
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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: 12.77 Å2
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Refine analyze | Luzzati coordinate error obs: 0.328 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→52.9 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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