+Open data
-Basic information
Entry | Database: PDB / ID: 3cry | ||||||
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Title | Gamma-glutamyl cyclotransferase | ||||||
Components | Gamma-glutamyl cyclotransferase | ||||||
Keywords | TRANSFERASE / enzyme / cyclotransferase / gamma-glutamyl / oxoproline | ||||||
Function / homology | Function and homology information gamma-glutamylcyclotransferase / gamma-glutamylcyclotransferase activity / Glutathione synthesis and recycling / release of cytochrome c from mitochondria / protein homodimerization activity / extracellular exosome / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Oakley, A.J. / Board, P.G. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2008 Title: The identification and structural characterization of C7orf24 as gamma-glutamyl cyclotransferase. An essential enzyme in the gamma-glutamyl cycle Authors: Oakley, A.J. / Yamada, T. / Liu, D. / Coggan, M. / Clark, A.G. / Board, P.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3cry.cif.gz | 92.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3cry.ent.gz | 70.1 KB | Display | PDB format |
PDBx/mmJSON format | 3cry.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3cry_validation.pdf.gz | 444.3 KB | Display | wwPDB validaton report |
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Full document | 3cry_full_validation.pdf.gz | 446.5 KB | Display | |
Data in XML | 3cry_validation.xml.gz | 19.2 KB | Display | |
Data in CIF | 3cry_validation.cif.gz | 28.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cr/3cry ftp://data.pdbj.org/pub/pdb/validation_reports/cr/3cry | HTTPS FTP |
-Related structure data
Related structure data | 2pn7C 2rbhSC 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: 21028.705 Da / Num. of mol.: 2 / Mutation: E98Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GGCT / Plasmid: pHUE / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O75223 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.76 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 50% PEG 4000, 0.2M ammonium acetate, 0.1M sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.95361 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Nov 15, 2007 / Details: mirrors |
Radiation | Monochromator: BEAMLINE OPTICS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95361 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→70.19 Å / Num. all: 38869 / Num. obs: 38628 / % possible obs: 99.4 % / Observed criterion σ(F): -2 / Observed criterion σ(I): -2 / Redundancy: 4.6 % / Biso Wilson estimate: 13.73 Å2 / Rmerge(I) obs: 0.092 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 1.7→1.8 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.419 / Mean I/σ(I) obs: 3.7 / Num. unique all: 5449 / % possible all: 97.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2RBH Resolution: 1.7→22.37 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.926 / SU B: 2.05 / SU ML: 0.07 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): -1 / σ(I): -1 / ESU R: 0.114 / ESU R Free: 0.115 / 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: 14.957 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→22.37 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.744 Å / Total num. of bins used: 20
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