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- PDB-1e1m: ADRENODOXIN REDUCTASE in complex with NADPH obtained by a soaking... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1e1m | ||||||
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Title | ADRENODOXIN REDUCTASE in complex with NADPH obtained by a soaking experiment | ||||||
![]() | ADRENODOXIN REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / NADPH / FLAVOENZYME / ELECTRON TRANSFERASE | ||||||
Function / homology | ![]() adrenodoxin-NADP+ reductase / NADPH-adrenodoxin reductase activity / ubiquinone biosynthetic process / steroid biosynthetic process / cholesterol metabolic process / electron transport chain / NADP binding / flavin adenine dinucleotide binding / mitochondrial inner membrane / mitochondrion Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ziegler, G.A. / Schulz, G.E. | ||||||
![]() | ![]() Title: Crystal Structures of Adrenodoxin Reductase in Complex with Nadp+ and Nadph Suggesting a Mechanism for the Electron Transfer of an Enzyme Family Authors: Ziegler, G.A. / Schulz, G.E. #1: ![]() Title: The Structure of Adrenodoxin Reductase of Mitochondrial P450 Systems: Electron Transfer for Steroid Biosynthesis Authors: Ziegler, G.A. / Vonrhein, C. / Hanukoglu, I. / Schulz, G.E. #2: Journal: FEBS Lett. / Year: 1999 Title: Chaperone-Assisted Expression of Authentic Bovine Adrenodoxin Reductase in Escherichia Coli Authors: Vonrhein, C. / Schmidt, U. / Ziegler, G.A. / Schweiger, S. / Hanukoglu, I. / Schulz, G.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 113.9 KB | Display | ![]() |
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PDB format | ![]() | 84.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1013.5 KB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 24.2 KB | Display | |
Data in CIF | ![]() | 35.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1e1kC ![]() 1e1lC ![]() 1e1nC ![]() 1cjcS 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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Unit cell |
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Components
#1: Protein | Mass: 50360.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-NAP / |
#4: Water | ChemComp-HOH / |
Sequence details | FIRST 32 RESIDUES OF SWISS-PROT SEQUENCE REFER TO A MITOCHONDRIAL LEADER SEQUENCE THAT WAS DELETED ...FIRST 32 RESIDUES OF SWISS-PROT SEQUENCE REFER TO A MITOCHONDR |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.19 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.50 | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Apr 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.847 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→18 Å / Num. obs: 47207 / % possible obs: 96.3 % / Redundancy: 3.2 % / Biso Wilson estimate: 18.8 Å2 / Rmerge(I) obs: 0.053 / Rsym value: 0.044 / Net I/σ(I): 12.3 |
Reflection shell | Resolution: 1.85→1.95 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 5 / Rsym value: 0.15 / % possible all: 96.3 |
Reflection | *PLUS Num. obs: 47193 / % possible obs: 96 % / Rmerge(I) obs: 0.044 |
Reflection shell | *PLUS % possible obs: 91 % / Rmerge(I) obs: 0.15 |
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Processing
Software | Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: ![]() Starting model: 1CJC Resolution: 1.85→18 Å / σ(F): 0
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Displacement parameters | Biso mean: 23.4 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.85→18 Å
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Refine LS restraints |
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Refinement | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 23 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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