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Yorodumi- PDB-2i89: Structure of septuple mutant of Rat Outer Mitochondrial Membrane ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2i89 | ||||||
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Title | Structure of septuple mutant of Rat Outer Mitochondrial Membrane Cytochrome B5 | ||||||
Components | Cytochrome b5 type B | ||||||
Keywords | ELECTRON TRANSPORT / CYTOCHROME B5 / HEME | ||||||
Function / homology | Function and homology information Sphingolipid de novo biosynthesis / Phase I - Functionalization of compounds / nitric-oxide synthase complex / nitrite reductase (NO-forming) activity / ubiquinol-cytochrome-c reductase activity / enzyme activator activity / nitric oxide biosynthetic process / mitochondrial outer membrane / intracellular membrane-bounded organelle / heme binding / metal ion binding Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 2.1 Å | ||||||
Authors | Terzyan, S. / Zhang, X.C. / Benson, D.R. / Wang, L. / Sun, N. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: A histidine/tryptophan pi-stacking interaction stabilizes the heme-independent folding core of microsomal apocytochrome b5 relative to that of mitochondrial apocytochrome b5. Authors: Wang, L. / Sun, N. / Terzyan, S. / Zhang, X. / Benson, D.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2i89.cif.gz | 97.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2i89.ent.gz | 76.3 KB | Display | PDB format |
PDBx/mmJSON format | 2i89.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2i89_validation.pdf.gz | 2.9 MB | Display | wwPDB validaton report |
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Full document | 2i89_full_validation.pdf.gz | 2.9 MB | Display | |
Data in XML | 2i89_validation.xml.gz | 22.5 KB | Display | |
Data in CIF | 2i89_validation.cif.gz | 28.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i8/2i89 ftp://data.pdbj.org/pub/pdb/validation_reports/i8/2i89 | HTTPS FTP |
-Related structure data
Related structure data | 1iccS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 10494.436 Da / Num. of mol.: 4 / Fragment: Water Soluble Domain / Mutation: R15H/A18S/E20S/I25L/I32L/L47R/L71S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Cyb5b / Plasmid: PET11A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P04166 #2: Chemical | #3: Chemical | ChemComp-HEM / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.66 % |
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Crystal grow | Temperature: 278 K / pH: 6.8 Details: PEG8K 30%, O.2M MgAc, 0.1M Pipes, VAPOR DIFFUSION, HANGING DROP, temperature 278K, pH 6.80 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: May 20, 2004 / Details: OSMIC BLUE OPTICS |
Radiation | Monochromator: OSMIC MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 19485 / % possible obs: 92.6 % / Observed criterion σ(I): -3 / Redundancy: 3.6 % / Biso Wilson estimate: 29.98 Å2 / Rmerge(I) obs: 0.099 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 2.1→2.18 Å / Rmerge(I) obs: 0.476 / Mean I/σ(I) obs: 2.6 / % possible all: 90.4 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 1ICC Resolution: 2.1→50 Å / Isotropic thermal model: ISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Bsol: 50.02 Å2 / ksol: 0.375 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.67 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→50 Å
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Refine LS restraints |
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Xplor file |
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