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Open data
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Basic information
Entry | Database: PDB / ID: 1irc | ||||||
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Title | CYSTEINE RICH INTESTINAL PROTEIN | ||||||
![]() | MYOGLOBIN (METAQUO) | ||||||
![]() | OXYGEN STORAGE / RESPIRATORY PROTEIN / HEME | ||||||
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 | ![]() | ||||||
![]() | Barrick, D.E. / Feese, M. | ||||||
![]() | ![]() Title: Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly. Authors: Barrick, D. #1: ![]() Title: Replacement of the Proximal Ligand of Sperm Whale Myoglobin with Free Imidazole in the Mutant His-93-->Gly Authors: Barrick, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 43.9 KB | Display | ![]() |
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PDB format | ![]() | 30.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 477.4 KB | Display | ![]() |
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Full document | ![]() | 484.6 KB | Display | |
Data in XML | ![]() | 5.8 KB | Display | |
Data in CIF | ![]() | 8 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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Unit cell |
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Components
#1: Protein | Mass: 17285.053 Da / Num. of mol.: 1 / Mutation: H93G Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene (production host): SPERM WHALE MYOGLOBIN SYNTHETIC GENE Production host: ![]() ![]() |
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#2: Chemical | ChemComp-HEM / |
#3: Chemical | ChemComp-IMD / |
#4: Water | ChemComp-HOH / |
Source details | THE PROTEIN WAS PRODUCED USING AN ESCHERICHIA COLI EXPRESSION SYSTEM OF SPRINGER AND SLIGAR [(1987) ...THE PROTEIN WAS PRODUCED USING AN ESCHERICHI |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.41 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.2 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 7676 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.033 |
Reflection | *PLUS Highest resolution: 2.17 Å / Lowest resolution: 26.6 Å / Num. measured all: 25555 |
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Processing
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Refinement | Resolution: 2.17→20 Å / Num. reflection obs: 7171 / σ(F): 0 / Stereochemistry target values: PROTGEO.DAT | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.17→20 Å
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.177 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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