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- PDB-2mgj: HIGH RESOLUTION CRYSTAL STRUCTURES OF FIVE DISTAL HISTIDINE MUTAN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2mgj | ||||||
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Title | HIGH RESOLUTION CRYSTAL STRUCTURES OF FIVE DISTAL HISTIDINE MUTANTS OF SPERM WHALE MYOGLOBIN | ||||||
![]() | MYOGLOBIN | ||||||
![]() | OXYGEN STORAGE | ||||||
Function / homology | ![]() Oxidoreductases; Acting on other nitrogenous compounds as donors / nitrite reductase activity / 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 | ![]() | ||||||
![]() | Quillin, M.L. / Arduini, R.M. / Phillips Jr., G.N. | ||||||
![]() | ![]() Title: High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. Authors: Quillin, M.L. / Arduini, R.M. / Olson, J.S. / Phillips Jr., G.N. #1: ![]() Title: Crystal Structure of Myoglobin from a Synthetic Gene Authors: Phillips Jr., G.N. / Arduini, R.M. / Springer, B.A. / Sligar, S.G. #2: ![]() Title: High-Level Expression of Sperm Whale Myoglobin in Escherichia Coli Authors: Springer, B.A. / Sligar, S.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 46.1 KB | Display | ![]() |
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PDB format | ![]() | 32.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1mobC ![]() 1mocC ![]() 1modC ![]() 2mgaC ![]() 2mgbC ![]() 2mgcC ![]() 2mgdC ![]() 2mgeC ![]() 2mgfC ![]() 2mggC ![]() 2mghC ![]() 2mgiC ![]() 2mgkC ![]() 2mglC ![]() 2mgmC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 17326.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-HEM / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.18 Å3/Da / Density % sol: 61.29 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 9 / Method: batch method / Details: micro seeding | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2 Å / % possible obs: 95.1 % / Rmerge(I) obs: 0.085 |
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Processing
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Refinement | Resolution: 2→5 Å /
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Refinement step | Cycle: LAST / Resolution: 2→5 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.156 / Rfactor Rwork: 0.156 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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