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- PDB-1ybv: STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADP... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ybv | ||||||
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Title | STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR | ||||||
![]() | TRIHYDROXYNAPHTHALENE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
Function / homology | ![]() tetrahydroxynaphthalene reductase / tetrahydroxynaphthalene reductase activity / melanin biosynthetic process Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Andersson, A. / Schneider, G. / Lindqvist, Y. | ||||||
![]() | ![]() Title: Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor. Authors: Andersson, A. / Jordan, D. / Schneider, G. / Lindqvist, Y. #1: ![]() Title: Crystallisation and Preliminary X-Ray Diffraction Study of 1,3,8-Trihydroxynaphthalene Reductase from Magnaporthe Grisea Authors: Andersson, A. / Jordan, D. / Schneider, G. / Valent, B. / Lindqvist, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 103.1 KB | Display | ![]() |
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PDB format | ![]() | 82 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 21.9 KB | Display | |
Data in CIF | ![]() | 25.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.999978, -0.004005, 0.005347), Vector: |
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Components
#1: Protein | Mass: 30151.643 Da / Num. of mol.: 2 / Mutation: P2A, S241V, A242Q, H247 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.55 Å3/Da / Density % sol: 58.5 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: Andersson, A., (1996) Proteins: Struct.,Funct., Genet., 24, 525. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Dec 16, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 19294 / % possible obs: 91.4 % / Observed criterion σ(I): 0 / Redundancy: 5.8 % / Rmerge(I) obs: 0.086 |
Reflection | *PLUS Highest resolution: 2.8 Å / Num. measured all: 111124 |
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Processing
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Refinement | Resolution: 2.8→8 Å / σ(F): 2 / Details: STRICT TWO-FOLD NON-CRYSTALLOGRAPHIC SYMMETRY
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Displacement parameters | Biso mean: 26.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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