+Open data
-Basic information
Entry | Database: PDB / ID: 3a30 | ||||||
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Title | E. coli Gsp amidase C59 acetate modification | ||||||
Components | Bifunctional glutathionylspermidine synthetase/amidase | ||||||
Keywords | Hydrolase / Ligase / Gsp amidase / ATP-binding / Multifunctional enzyme / Nucleotide-binding | ||||||
Function / homology | Function and homology information glutathionylspermidine amidase / glutathionylspermidine synthase / glutathionylspermidine amidase activity / glutathionylspermidine synthase activity / spermidine metabolic process / glutathione metabolic process / ATP binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Pai, C.-H. / Ko, T.-P. / Chiang, B.-Y. / Lin, C.-H. / Wang, A.H.-J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2010 Title: Protein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetASE/amidase in redox regulation Authors: Chiang, B.-Y. / Chen, T.-C. / Pai, C.-H. / Chou, C.-C. / Chen, H.-H. / Ko, T.-P. / Hsu, W.-H. / Chang, C.-Y. / Wu, W.-F. / Wang, A.H.-J. / Lin, C.-H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3a30.cif.gz | 52.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3a30.ent.gz | 36.6 KB | Display | PDB format |
PDBx/mmJSON format | 3a30.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a3/3a30 ftp://data.pdbj.org/pub/pdb/validation_reports/a3/3a30 | HTTPS FTP |
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-Related structure data
Related structure data | 3a2zC 2iobS 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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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 22293.912 Da / Num. of mol.: 1 / Fragment: residues 1-197 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: gsp, b2988, JW2956 / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: P0AES0, glutathionylspermidine synthase, glutathionylspermidine amidase |
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#2: Chemical | ChemComp-ACT / |
#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: 2.39 Å3/Da / Density % sol: 48.52 % |
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Crystal grow | Temperature: 298 K / Method: evaporation / pH: 4.5 Details: 0.1M acetate, 0.8M NaH2PO4, 1.2M K2HPO4, pH 4.5, EVAPORATION, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13C1 |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.2→30 Å / Num. obs: 11604 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 10.1 % / Rmerge(I) obs: 0.092 / Net I/σ(I): 34.8 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 10.3 % / Rmerge(I) obs: 0.609 / Mean I/σ(I) obs: 5.9 / Num. unique all: 1114 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2iob Resolution: 2.2→25.25 Å / Occupancy max: 1 / Occupancy min: 0.5 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 37.67 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso max: 68.35 Å2 / Biso mean: 24.918 Å2 / Biso min: 7.61 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→25.25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.28 Å
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Xplor file |
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