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Yorodumi- PDB-1e1n: Structure of adrenodoxin reductase at 2.4 Angstrom in crystal form A' -
+Open data
-Basic information
Entry | Database: PDB / ID: 1e1n | ||||||
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Title | Structure of adrenodoxin reductase at 2.4 Angstrom in crystal form A' | ||||||
Components | ADRENODOXIN REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / FLAVOENZYME / ELECTRON TRANSFERASE | ||||||
Function / homology | Function and homology information adrenodoxin-NADP+ reductase / NADPH-adrenodoxin reductase activity / ubiquinone biosynthetic process / steroid biosynthetic process / electron transport chain / cholesterol metabolic process / flavin adenine dinucleotide binding / NADP binding / mitochondrial inner membrane / mitochondrion Similarity search - Function | ||||||
Biological species | BOS TAURUS (cattle) | ||||||
Method | X-RAY DIFFRACTION / MAD / Resolution: 2.4 Å | ||||||
Authors | Ziegler, G.A. / Schulz, G.E. | ||||||
Citation | Journal: Biochemistry / Year: 2000 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: Journal: J.Mol.Biol. / Year: 1999 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e1n.cif.gz | 100 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e1n.ent.gz | 80.3 KB | Display | PDB format |
PDBx/mmJSON format | 1e1n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e1/1e1n ftp://data.pdbj.org/pub/pdb/validation_reports/e1/1e1n | 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: 50360.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BOS TAURUS (cattle) / Tissue: STEROIDOGENIC TISSUES STEROIDOGENIC TISSUES / Cellular location: MITOCHONDRIAL MATRIX / Organelle: MITOCHONDRIAMitochondrion / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P08165 |
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#2: Chemical | ChemComp-FAD / |
#3: Water | ChemComp-HOH / |
Sequence details | FIRST 32 RESIDUES OF SWISS-PROT SEQUENCE REFER TO A MITOCHONDR |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.42 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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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: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Date: Jan 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→32.3 Å / Num. obs: 17479 / % possible obs: 74.4 % / Redundancy: 2.4 % / Biso Wilson estimate: 32.8 Å2 / Rmerge(I) obs: 0.057 / Rsym value: 0.048 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 2.35→2.48 Å / Redundancy: 1.2 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 5 / Rsym value: 0.12 / % possible all: 36.8 |
Reflection shell | *PLUS % possible obs: 36.8 % |
-Processing
Software | Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MAD / Resolution: 2.4→29 Å / σ(F): 0 Details: SMALL DOMAIN MOVEMENT AGAINST OTHER NATIVE STRUCTURES
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Displacement parameters | Biso mean: 43.1 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→29 Å
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Refine LS restraints |
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