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Yorodumi- PDB-4gdx: Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutama... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4gdx | ||||||
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Title | Crystal Structure of Human Gamma-Glutamyl Transpeptidase--Glutamate complex | ||||||
Components | (Gamma-glutamyltranspeptidase 1 ...) x 2 | ||||||
Keywords | HYDROLASE / product-enzyme complex / Ntn-hydrolase family / glycoprotein / N-glycosylation / cell surface | ||||||
Function / homology | Function and homology information leukotriene-C4 hydrolase / peptidyltransferase activity / leukotriene-C(4) hydrolase / leukotriene D4 biosynthetic process / Defective GGT1 causes GLUTH / Defective GGT1 in aflatoxin detoxification causes GLUTH / LTC4-CYSLTR mediated IL4 production / Glutathione synthesis and recycling / peptide modification / gamma-glutamyltransferase ...leukotriene-C4 hydrolase / peptidyltransferase activity / leukotriene-C(4) hydrolase / leukotriene D4 biosynthetic process / Defective GGT1 causes GLUTH / Defective GGT1 in aflatoxin detoxification causes GLUTH / LTC4-CYSLTR mediated IL4 production / Glutathione synthesis and recycling / peptide modification / gamma-glutamyltransferase / glutathione gamma-glutamate hydrolase / glutathione hydrolase activity / leukotriene C4 gamma-glutamyl transferase activity / glutathione catabolic process / glutathione biosynthetic process / glutamate metabolic process / leukotriene metabolic process / Aflatoxin activation and detoxification / cysteine biosynthetic process / Synthesis of Leukotrienes (LT) and Eoxins (EX) / regulation of immune system process / Paracetamol ADME / zymogen activation / amino acid metabolic process / fatty acid metabolic process / regulation of inflammatory response / spermatogenesis / proteolysis / extracellular space / extracellular exosome / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.67 Å | ||||||
Authors | West, M.B. / Chen, Y. / Wickham, S. / Heroux, A. / Cahill, K. / Hanigan, M.H. / Mooers, B.H.M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2013 Title: Novel Insights into Eukaryotic gamma-Glutamyltranspeptidase 1 from the Crystal Structure of the Glutamate-bound Human Enzyme. Authors: West, M.B. / Chen, Y. / Wickham, S. / Heroux, A. / Cahill, K. / Hanigan, M.H. / Mooers, B.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4gdx.cif.gz | 231.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4gdx.ent.gz | 186.3 KB | Display | PDB format |
PDBx/mmJSON format | 4gdx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gd/4gdx ftp://data.pdbj.org/pub/pdb/validation_reports/gd/4gdx | HTTPS FTP |
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-Related structure data
Related structure data | 4gg2C 2dbuS 4gg3 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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Unit cell |
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-Components
-Gamma-glutamyltranspeptidase 1 ... , 2 types, 2 molecules AB
#1: Protein | Mass: 40874.965 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GGT, GGT1 / Production host: PICHIA (fungus) References: UniProt: P19440, gamma-glutamyltransferase, glutathione gamma-glutamate hydrolase, leukotriene-C4 hydrolase |
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#2: Protein | Mass: 20556.938 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GGT, GGT1 / Production host: PICHIA (fungus) References: UniProt: P19440, gamma-glutamyltransferase, glutathione gamma-glutamate hydrolase, leukotriene-C4 hydrolase |
-Sugars , 1 types, 6 molecules
#3: Sugar | ChemComp-NAG / |
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-Non-polymers , 4 types, 603 molecules
#4: Chemical | #5: Chemical | ChemComp-NA / | #6: Chemical | ChemComp-GLU / | #7: Water | ChemComp-HOH / | |
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-Details
Sequence details | THE UNP P19440 HAS VAL272 WHEN THIS STRUCTURE HAS ALA272. ALA272 IS A NATURAL VARIANT ON THIS HUMAN ...THE UNP P19440 HAS VAL272 WHEN THIS STRUCTURE HAS ALA272. ALA272 IS A NATURAL VARIANT ON THIS HUMAN PROTEIN. THE SEQUENCE OF THIS VARIANT IS GIVEN BY GENBANK AAA52546.1 |
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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: 2.81 Å3/Da / Density % sol: 56.22 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 17.5% PEG3350, 100 mM Ammonium chloride, 0.5 mM L-glutamate, and 100 mM Na:Cacodylate pH 6.0 , VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 18, 2011 Details: A Si-111 double crystal monochromator that provides a broad range 7-15 keV (0.8 2-1.8 ) x-rays. The undulator beam is focused vertically by a Rh-coated mirror. |
Radiation | Monochromator: A Si-111 double crystal monochromator that provides a broad range 7-15 keV (0.82-1.8 ) x-rays. The undulator beam is focused vertically by a Rh-coated mirror. Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.67→47.07 Å / Num. all: 70751 / Num. obs: 70751 / % possible obs: 98.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 6.3 % / Biso Wilson estimate: 17.2 Å2 / Rmerge(I) obs: 0.076 / Rsym value: 0.076 / Net I/σ(I): 16.2 |
Reflection shell | Resolution: 1.67→1.76 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.74 / Mean I/σ(I) obs: 2.1 / Rsym value: 0.74 / % possible all: 90.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 2DBU Resolution: 1.67→47.07 Å / SU ML: 0.15 / σ(F): 1.34 / Phase error: 17.18 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.67→47.07 Å
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Refine LS restraints |
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LS refinement shell |
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