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Yorodumi- PDB-1g0o: STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADP... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1g0o | ||||||
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Title | STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND PYROQUILON | ||||||
Components | TRIHYDROXYNAPHTHALENE REDUCTASE | ||||||
Keywords | oxidoreductase/oxidoreductase INHIBITOR / Protein-NADPH-active site inhibitor complex / dinucleotide binding fold / oxidoreductase / short chain dehydrogenase / oxidoreductase-oxidoreductase INHIBITOR complex | ||||||
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: 1.7 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 | 1g0o.cif.gz | 245.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g0o.ent.gz | 197.1 KB | Display | PDB format |
PDBx/mmJSON format | 1g0o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g0/1g0o ftp://data.pdbj.org/pub/pdb/validation_reports/g0/1g0o | HTTPS FTP |
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-Related 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: 30177.682 Da / Num. of mol.: 4 / 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 | ChemComp-NDP / #3: Chemical | ChemComp-PYQ / #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: 2.72 Å3/Da / Density % sol: 54.86 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 274 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG 6K, glycerol, Hepes-NaOH, 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: Sep 29, 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: 1.7→30 Å / Num. all: 141563 / Num. obs: 543990 / % possible obs: 97.2 % / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 24.5 |
Reflection shell | Resolution: 1.7→1.73 Å / Redundancy: 2 % / Rmerge(I) obs: 0.227 / Num. unique all: 6244 / % possible all: 86.9 |
Reflection | *PLUS Num. obs: 141563 / Num. measured all: 543990 |
Reflection shell | *PLUS % possible obs: 86.9 % |
-Processing
Software |
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Refinement | Resolution: 1.7→8 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.7→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: 1.7 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.176 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS Type: x_bond_d / Dev ideal: 0.01 |