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Yorodumi- PDB-1b1c: CRYSTAL STRUCTURE OF THE FMN-BINDING DOMAIN OF HUMAN CYTOCHROME P... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1b1c | ||||||
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Title | CRYSTAL STRUCTURE OF THE FMN-BINDING DOMAIN OF HUMAN CYTOCHROME P450 REDUCTASE AT 1.93A RESOLUTION | ||||||
Components | PROTEIN (NADPH-CYTOCHROME P450 REDUCTASE) | ||||||
Keywords | OXIDOREDUCTASE / FLAVOPROTEIN / CYTOCHROME P450 REDUCTASE / P450 REDUCTASE / FMN-BINDING DOMAIN / FMN | ||||||
Function / homology | Function and homology information Cytochrome P450 - arranged by substrate type / positive regulation of monooxygenase activity / cellular organofluorine metabolic process / NADPH-hemoprotein reductase / NADPH-hemoprotein reductase activity / xenobiotic metabolic process / response to hormone / electron transport chain / FMN binding / NADP binding ...Cytochrome P450 - arranged by substrate type / positive regulation of monooxygenase activity / cellular organofluorine metabolic process / NADPH-hemoprotein reductase / NADPH-hemoprotein reductase activity / xenobiotic metabolic process / response to hormone / electron transport chain / FMN binding / NADP binding / flavin adenine dinucleotide binding / intracellular membrane-bounded organelle / endoplasmic reticulum membrane / membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MIRAS / Resolution: 1.93 Å | ||||||
Authors | Zhao, Q. / Modi, S. / Smith, G. / Paine, M. / Mcdonagh, P.D. / Wolf, C.R. / Tew, D. / Lian, L.-Y. / Roberts, G.C.K. / Driessen, H.P.C. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Authors: Zhao, Q. / Modi, S. / Smith, G. / Paine, M. / McDonagh, P.D. / Wolf, C.R. / Tew, D. / Lian, L.Y. / Roberts, G.C. / Driessen, H.P. #1: Journal: J.Struct.Biol. / Year: 1996 Title: Crystallization and Preliminary X-Ray Diffraction Studies of Human Cytochrome P450 Reductase Authors: Zhao, Q. / Smith, G. / Modi, S. / Paine, M. / Wolf, R.C. / Tew, D. / Lian, L.Y. / Primrose, W.U. / Roberts, G.C. / Driessen, H.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b1c.cif.gz | 48.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b1c.ent.gz | 33.1 KB | Display | PDB format |
PDBx/mmJSON format | 1b1c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1b1c_validation.pdf.gz | 771.3 KB | Display | wwPDB validaton report |
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Full document | 1b1c_full_validation.pdf.gz | 776.7 KB | Display | |
Data in XML | 1b1c_validation.xml.gz | 10.3 KB | Display | |
Data in CIF | 1b1c_validation.cif.gz | 13.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b1/1b1c ftp://data.pdbj.org/pub/pdb/validation_reports/b1/1b1c | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20380.314 Da / Num. of mol.: 1 / Fragment: FMN-BINDING DOMAIN / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Plasmid: PMP CLONED INTO PET15B / References: UniProt: P16435, NADPH-hemoprotein reductase |
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#2: Chemical | ChemComp-CA / |
#3: Chemical | ChemComp-FMN / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.82 % | ||||||||||||||||||||||||
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Crystal grow | pH: 7 Details: 18-20% (W/V) PEG400, 100 MM HEPES (PH6.8-7.2), 200 MM CACL2 4 DEGREES C, pH 7.0 | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: batch method / Details: Zhao, Q., (1996) J.Struct.Biol., 116, 320. / PH range low: 7.2 / PH range high: 6.8 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.93→19.45 Å / Num. obs: 13289 / % possible obs: 89.2 % / Observed criterion σ(I): 3 / Redundancy: 3.9 % / Rmerge(I) obs: 0.082 |
Reflection shell | Highest resolution: 1.93 Å / Rmerge(I) obs: 0.193 / % possible all: 72.9 |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS / Resolution: 1.93→19.45 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT, EXCEPT LAST 2 PASSES / σ(F): 0
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Refine analyze | Luzzati coordinate error obs: 0.22 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.93→19.45 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.1973 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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