+Open data
-Basic information
Entry | Database: PDB / ID: 3ozz | ||||||
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Title | Structure of a cytochrome b5 core-swap mutant | ||||||
Components | Cytochrome b5 | ||||||
Keywords | ELECTRON TRANSPORT / HIBRID CYTOCHROME B5 / HEME | ||||||
Function / homology | Function and homology information Vitamin C (ascorbate) metabolism / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / mitochondrial outer membrane / intracellular membrane-bounded organelle / heme binding / endoplasmic reticulum membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Terzyan, S. / Parthasarathy, S. / Zhang, X.C. / Benson, D. | ||||||
Citation | Journal: To be Published Title: Structure of a cytochrome b5 core-swap mutant Authors: Parthasarathy, S. / Terzyan, S. / Zhang, X.C. / Benson, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ozz.cif.gz | 36.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ozz.ent.gz | 24 KB | Display | PDB format |
PDBx/mmJSON format | 3ozz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oz/3ozz ftp://data.pdbj.org/pub/pdb/validation_reports/oz/3ozz | HTTPS FTP |
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-Related structure data
Related structure data | 1awpS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 9446.489 Da / Num. of mol.: 1 Fragment: N-TERMINAL HEME-BINDING DOMAIN (unp residues 8-89) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Gene: CYB5, CYB5A, Cyb5b, Cyb5m, Omb5 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): Bl21 / References: UniProt: P00171 |
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#2: Chemical | ChemComp-HEM / |
#3: 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: 2.1 Å3/Da / Density % sol: 41.55 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion / pH: 7 Details: 30% PEG8000, 0.2M MgAc, 0.1M Pipes, pH 7.0, VAPOR DIFFUSION, temperature 277K |
-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jan 1, 2007 / Details: mirrors |
Radiation | Monochromator: Osmic Blue optics / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 8707 / % possible obs: 98.4 % / Observed criterion σ(F): -3 / Redundancy: 4 % / Biso Wilson estimate: 17.87 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 24.5 |
Reflection shell | Resolution: 1.7→1.76 Å / Rmerge(I) obs: 0.152 / Mean I/σ(I) obs: 8.2 / % possible all: 95.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1AWP Resolution: 1.7→50 Å / Isotropic thermal model: Anisotropic Overall Temp. factor / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 17.72 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→50 Å
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Refine LS restraints |
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