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Open data
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Basic information
Entry | Database: PDB / ID: 1mwd | ||||||
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Title | WILD TYPE DEOXY MYOGLOBIN | ||||||
![]() | PROTEIN (MYOGLOBIN) | ||||||
![]() | OXYGEN STORAGE/TRANSPORT / OXYGEN STORAGE / DEOXY MYOGLOBIN / OXYGEN STORAGE-TRANSPORT COMPLEX | ||||||
Function / homology | ![]() Intracellular oxygen transport / Oxidoreductases; Acting on other nitrogenous compounds as donors / nitrite reductase activity / oxygen transport / sarcoplasm / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / removal of superoxide radicals / oxygen carrier activity / peroxidase activity / oxygen binding ...Intracellular oxygen transport / Oxidoreductases; Acting on other nitrogenous compounds as donors / nitrite reductase activity / oxygen transport / sarcoplasm / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / removal of superoxide radicals / oxygen carrier activity / peroxidase activity / oxygen binding / heme binding / extracellular exosome / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Murshudov, G.N. / Krzywda, S. / Brzozowski, A.M. / Jaskolski, M. / Scott, E.E. / Klizas, A.A. / Gibson, Q.H. / Olson, J.S. / Wilkinson, A.J. | ||||||
![]() | ![]() Title: Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution. Authors: Krzywda, S. / Murshudov, G.N. / Brzozowski, A.M. / Jaskolski, M. / Scott, E.E. / Klizas, S.A. / Gibson, Q.H. / Olson, J.S. / Wilkinson, A.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.2 KB | Display | ![]() |
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PDB format | ![]() | 65.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 16983.445 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: MYOGLOBIN / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.46 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||
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Crystal grow | pH: 7.1 Details: 0.1 PHOSPHATE BUFFER 72-80% SATURATED AMMONIUM SULPHATE, pH 7.1 | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 150 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→24 Å / Num. obs: 42068 / % possible obs: 96.5 % / Redundancy: 7.9 % / Biso Wilson estimate: 26.5 Å2 / Rsym value: 0.04 / Net I/σ(I): 21.4 |
Reflection | *PLUS Highest resolution: 1.8 Å / Rmerge(I) obs: 0.04 |
Reflection shell | *PLUS Rmerge(I) obs: 0.291 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 1.8→24 Å / SU B: 2.58 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 31 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→24 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / σ(F): 0 / % reflection Rfree: 5 % / Rfactor obs: 0.196 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 31 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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