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Open data
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Basic information
Entry | Database: PDB / ID: 1cyo | |||||||||
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Title | BOVINE CYTOCHROME B(5) | |||||||||
![]() | CYTOCHROME B5 | |||||||||
![]() | ELECTRON TRANSPORT | |||||||||
Function / homology | ![]() 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 | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Durley, R.C.E. / Mathews, F.S. | |||||||||
![]() | ![]() Title: Refinement and structural analysis of bovine cytochrome b5 at 1.5 A resolution. Authors: Durley, R.C. / Mathews, F.S. #1: ![]() Year: 1985 Title: Cytochrome B5 and Cytochrome B5 Reductase from a Chemical and X-Ray Diffraction Viewpoint Authors: Mathews, F.S. / Czerwinski, E.W. #2: ![]() Title: The X-Ray Crystallographic Structure of Calf Liver Cytochrome B5 Authors: Mathews, F.S. / Czerwinski, E.W. / Argos, P. #3: ![]() Title: The Structure of Cytochrome B5 at 2.0 Angstroms Resolution Authors: Mathews, F.S. / Argos, P. / Levine, M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 34.4 KB | Display | ![]() |
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PDB format | ![]() | 22.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 787.7 KB | Display | ![]() |
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Full document | ![]() | 788.7 KB | Display | |
Data in XML | ![]() | 7.7 KB | Display | |
Data in CIF | ![]() | 10.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Atom site foot note | 1: ALTERNATE POSITIONS WERE REFINED FOR THE SIDE-CHAINS OF RESIDUES GLU 48, VAL 61, GLU 69, AND ILE 75. |
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Components
#1: Protein | Mass: 10651.721 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-HEM / |
#3: Water | ChemComp-HOH / |
Compound details | THE PROTEIN WAS SOLUBILIZE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.02 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.1 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 2.2 Å / Num. obs: 9843 / % possible obs: 99.2 % / Num. measured all: 13356 |
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Reflection shell | *PLUS Highest resolution: 1.5 Å / Lowest resolution: 1.6 Å / % possible obs: 16.5 % |
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Processing
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Refinement | Resolution: 1.5→10 Å /
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Refinement step | Cycle: LAST / Resolution: 1.5→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rwork: 0.164 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_bond_d / Dev ideal: 0.009 |