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Yorodumi- PDB-1g0n: STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADP... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1g0n | ||||||
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Title | STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND 4,5,6,7-TETRACHLORO-PHTHALIDE | ||||||
Components | TRIHYDROXYNAPHTHALENE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / Protein-NADPH-active site inhibitor complex / diuncleotide binding fold / short chain dehydrogenase | ||||||
Function / homology | Function and homology information tetrahydroxynaphthalene reductase / tetrahydroxynaphthalene reductase activity / melanin biosynthetic process Similarity search - Function | ||||||
Biological species | Magnaporthe grisea (fungus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Liao, D. / Basarab, G.S. / Gatenby, A.A. / Valent, B. / Jordan, D.B. | ||||||
Citation | Journal: Structure / Year: 2001 Title: Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis. Authors: Liao, D. / Basarab, G.S. / Gatenby, A.A. / Valent, B. / Jordan, D.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g0n.cif.gz | 121.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g0n.ent.gz | 94.3 KB | Display | PDB format |
PDBx/mmJSON format | 1g0n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1g0n_validation.pdf.gz | 602.1 KB | Display | wwPDB validaton report |
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Full document | 1g0n_full_validation.pdf.gz | 612.3 KB | Display | |
Data in XML | 1g0n_validation.xml.gz | 13.8 KB | Display | |
Data in CIF | 1g0n_validation.cif.gz | 21.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g0/1g0n ftp://data.pdbj.org/pub/pdb/validation_reports/g0/1g0n | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a homo tetramer. The two molecules in the asymmetric unit represent half of the biological assembly. The tetramer has a 222 symmetry / The following transformation should be applied to both chain A and chain B to generate the tetramer. Rotation matrix: -0.500 -0.866 0.00 -0.866 0.500 0.00 0.00 0.00 -1.00 Translation vector: 214.21, 123.66, 24.31 |
-Components
#1: Protein | Mass: 30177.682 Da / Num. of mol.: 2 / Mutation: S241V, A242Q, H247R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Magnaporthe grisea (fungus) / Plasmid: PTHNR2 / Production host: Escherichia coli (E. coli) References: UniProt: Q12634, tetrahydroxynaphthalene reductase #2: Chemical | #3: Chemical | ChemComp-PHH / | #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: 3.43 Å3/Da / Density % sol: 64.15 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 274 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG 6K, glycerol, Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 274K | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 102 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.54 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Aug 26, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 54812 / Num. obs: 208682 / % possible obs: 96.5 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 15.1 |
Reflection shell | Resolution: 2→2.03 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.351 / Num. unique all: 2189 / % possible all: 76.4 |
Reflection | *PLUS Num. obs: 54812 / Num. measured all: 208682 |
Reflection shell | *PLUS % possible obs: 76.4 % |
-Processing
Software |
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Refinement | Resolution: 2→8 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber Details: Only one monomer of the dimer in the asymmetric unit has the electron density for the inhibitor.
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | |||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 8 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor obs: 0.195 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS |