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Open data
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Basic information
Entry | Database: PDB / ID: 1f3p | ||||||
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Title | FERREDOXIN REDUCTASE (BPHA4)-NADH COMPLEX | ||||||
![]() | FERREDOXIN REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / Rossmann fold | ||||||
Function / homology | ![]() oxidoreductase activity, acting on NAD(P)H / flavin adenine dinucleotide binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Senda, T. / Yamada, T. / Sakurai, N. / Kubota, M. / Nishizaki, T. / Masai, E. / Fukuda, M. / Mitsuidagger, Y. | ||||||
![]() | ![]() Title: Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase. Authors: Senda, T. / Yamada, T. / Sakurai, N. / Kubota, M. / Nishizaki, T. / Masai, E. / Fukuda, M. / Mitsuidagger, Y. #1: ![]() Title: Identification of the bphA4 gene encoding ferredoxin reductase involved in biphenyl and polychlorinated biphenyl degradation in Pseudomonas sp. strain KKS102. Authors: Kikuchi, Y. / Nagata, Y. / Hinata, M. / Kimbara, K. / Fukuda, M. / Yano, Y. / Takagi, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 91.3 KB | Display | ![]() |
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PDB format | ![]() | 69 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 551.4 KB | Display | ![]() |
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Full document | ![]() | 565.9 KB | Display | |
Data in XML | ![]() | 11.6 KB | Display | |
Data in CIF | ![]() | 17.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Details | The biological assembly seems to be a dimer. However, the dimer form can not be indentified in the crystal. |
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Components
#1: Protein | Mass: 43221.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q52437, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen |
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#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-NAD / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.91 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 2.0M Sodium formate, 100mM Na acetate buffer, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 5.4 / Details: Yamada, T., (2000) Protein Pept.Lett., 7, 277. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: WEISSENBERG / Detector: DIFFRACTOMETER / Date: Dec 11, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→38 Å / Num. all: 133802 / Num. obs: 133802 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Biso Wilson estimate: 41.4 Å2 / Rmerge(I) obs: 0.085 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 6 % / Rmerge(I) obs: 0.478 / % possible all: 99.2 |
Reflection | *PLUS Num. obs: 19786 / Num. measured all: 133802 |
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Processing
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Refinement | Resolution: 2.4→38 Å / σ(F): 1 / σ(I): 1 / Stereochemistry target values: Engh & Huber / Details: Used bulk solvent correction.
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Refinement step | Cycle: LAST / Resolution: 2.4→38 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 38 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor obs: 0.206 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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