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- PDB-1moa: A NOVEL SITE-DIRECTED MUTANT OF MYOGLOBIN WITH AN UNUSUALLY HIGH ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1moa | ||||||
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Title | A NOVEL SITE-DIRECTED MUTANT OF MYOGLOBIN WITH AN UNUSUALLY HIGH O2 AFFINITY AND LOW AUTOOXIDATION RATE | ||||||
![]() | 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. / Phillips Jr., G.N. | ||||||
![]() | ![]() Title: A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate. Authors: Carver, T.E. / Brantley Jr., R.E. / Singleton, E.W. / Arduini, R.M. / Quillin, M.L. / Phillips Jr., G.N. / Olson, J.S. #1: ![]() Title: Structural and Functional Effects of Apolar Mutations of Val68(E11) in Myoglobin Authors: Quillin, M.L. / Li, T. / Olson, J.S. / Phillips Jr., G.N. / Dou, Y. / Ikeda-Saito, M. / Regan, R. / Carlson, M. / Gibson, Q.H. / Li, H. / Elber, R. #2: ![]() 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. #3: ![]() Title: Crystal Structure of Myoglobin from a Synthetic Gene Authors: Phillips Jr., G.N. / Arduini, R.M. / 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 | ![]() | 46.8 KB | Display | ![]() |
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PDB format | ![]() | 32.6 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 17399.180 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: 3.16 Å3/Da / Density % sol: 61.13 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 9 / Method: vapor diffusion, hanging dropDetails: Phillips Junior, G.N., (1990) Proteins.Struct.,Funct., Genet., 7, 358. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
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Refinement | Rfactor Rwork: 0.1546 / Rfactor obs: 0.1546 / Highest resolution: 1.9 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.9 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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