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Yorodumi- PDB-5v36: 1.88 Angstrom Resolution Crystal Structure of Glutathione Reducta... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 5v36 | ||||||
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| Title | 1.88 Angstrom Resolution Crystal Structure of Glutathione Reductase from Streptococcus mutans UA159 in Complex with FAD | ||||||
Components | Glutathione reductase | ||||||
Keywords | HYDROLASE / OXIDOREDUCTASE / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID / Glutathione Reductase / FAD | ||||||
| Function / homology | Function and homology informationglutathione-disulfide reductase / glutathione-disulfide reductase (NADPH) activity / glutathione metabolic process / cell redox homeostasis / NADP binding / flavin adenine dinucleotide binding / cellular response to oxidative stress / cytosol Similarity search - Function | ||||||
| Biological species | Streptococcus mutans serotype c (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.88 Å | ||||||
Authors | Minasov, G. / Shuvalova, L. / Dubrovska, I. / Kiryukhina, O. / Grimshaw, S. / Kwon, K. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID) | ||||||
Citation | Journal: Microbiol Resour Announc / Year: 2025Title: Structural genomics of bacterial drug targets: Application of a high-throughput pipeline to solve 58 protein structures from pathogenic and related bacteria. Authors: Inniss, N.L. / Minasov, G. / Chang, C. / Tan, K. / Kim, Y. / Maltseva, N. / Stogios, P. / Filippova, E. / Michalska, K. / Osipiuk, J. / Jaroszewki, L. / Godzik, A. / Savchenko, A. / ...Authors: Inniss, N.L. / Minasov, G. / Chang, C. / Tan, K. / Kim, Y. / Maltseva, N. / Stogios, P. / Filippova, E. / Michalska, K. / Osipiuk, J. / Jaroszewki, L. / Godzik, A. / Savchenko, A. / Joachimiak, A. / Anderson, W.F. / Satchell, K.J.F. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 5v36.cif.gz | 403.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5v36.ent.gz | 330 KB | Display | PDB format |
| PDBx/mmJSON format | 5v36.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v3/5v36 ftp://data.pdbj.org/pub/pdb/validation_reports/v3/5v36 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 5tr3C ![]() 5tv2C ![]() 5ty0C ![]() 5u1oSC ![]() 5u2gC ![]() 5u47C ![]() 5ue1C ![]() 5umeC ![]() 5us8C ![]() 5uswC ![]() 5usxC ![]() 5utxC ![]() 5uu6C ![]() 5uwyC ![]() 5ux9C ![]() 5vdnC ![]() 5vfbC ![]() 5vh6C ![]() 5wi5C ![]() 5wp0C ![]() 6aonC ![]() 6aooC ![]() 6awaC ![]() 6aziC ![]() 6b4oC ![]() 6b5fC ![]() 6b8dC ![]() 6balC ![]() 6bk7C ![]() 6blbC ![]() 6bq9C ![]() 6bz0C ![]() 6c8qC ![]() 6cmzC ![]() 6cn1C ![]() 6czpC ![]() 6e5yC ![]() 6muqC ![]() 6n0iC ![]() 6n7fC ![]() 6nfpC ![]() 6nkjC ![]() 6po4C ![]() 6pu9C ![]() 6puaC ![]() 6pxaC ![]() 6w2zC ![]() 9bznC ![]() 9bzqC ![]() 9bzrC S: Starting model for refinement C: citing same article ( |
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| Similar structure data | |
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Links
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Assembly
| Deposited unit | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
-Protein / Sugars , 2 types, 3 molecules AB

| #1: Protein | Mass: 49307.426 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (bacteria)Strain: ATCC 700610 / UA159 / Gene: gshR, SMU_838 / Plasmid: pMCSG53 / Production host: ![]() References: UniProt: Q8DUR5, adenosylhomocysteinase, glutathione-disulfide reductase #8: Sugar | ChemComp-BDF / | |
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-Non-polymers , 7 types, 1082 molecules 












| #2: Chemical | | #3: Chemical | #4: Chemical | ChemComp-CL / #5: Chemical | ChemComp-SO4 / #6: Chemical | ChemComp-GOL / #7: Chemical | ChemComp-EPE / | #9: Water | ChemComp-HOH / | |
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-Details
| Has protein modification | Y |
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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: 2.8 Å3/Da / Density % sol: 56.1 % |
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| Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: Protein: 8.0 mg/ml, 0.5M Sodium chloride, 0.01M Tris HCl (pH 8.3), 1.mM FAD; Screen: Classics II (A5), 2M Ammonium sulfate, 0.1 HEPES (pH 7.5); Cryo: 4M Ammonium sulfate : 50% Sucrose (1:1) |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å |
| Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 23, 2017 / Details: C(111) |
| Radiation | Monochromator: beryllium lenses / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97872 Å / Relative weight: 1 |
| Reflection | Resolution: 1.88→30 Å / Num. obs: 95700 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 15.1 % / Biso Wilson estimate: 27.8 Å2 / Rmerge(I) obs: 0.076 / Rpim(I) all: 0.02 / Rsym value: 0.076 / Χ2: 1.003 / Net I/σ(I): 35.2 |
| Reflection shell | Resolution: 1.88→1.91 Å / Redundancy: 14 % / Rmerge(I) obs: 0.775 / Mean I/σ(I) obs: 3.8 / Num. unique obs: 4685 / CC1/2: 0.888 / Rpim(I) all: 0.21 / Rsym value: 0.775 / Χ2: 0.997 / % possible all: 99.7 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 5U1O Resolution: 1.88→29.81 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.967 / SU B: 4.126 / SU ML: 0.067 / Cross valid method: THROUGHOUT / ESU R: 0.109 / ESU R Free: 0.102 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 29.111 Å2
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| Refinement step | Cycle: 1 / Resolution: 1.88→29.81 Å
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| Refine LS restraints |
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Streptococcus mutans serotype c (bacteria)
X-RAY DIFFRACTION
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