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- PDB-1gn3: H145Q mutant of Mycobacterium tuberculosis iron-superoxide dismutase. -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gn3 | ||||||
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Title | H145Q mutant of Mycobacterium tuberculosis iron-superoxide dismutase. | ||||||
![]() | SUPEROXIDE DISMUTASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
Function / homology | ![]() detoxification / Tolerance of reactive oxygen produced by macrophages / superoxide dismutase / superoxide dismutase activity / manganese ion binding / response to oxidative stress / periplasmic space / iron ion binding / extracellular region / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Bunting, K.A. / Cooper, J.B. / Badasso, M.O. / Tickle, I.J. / Newton, M. / Wood, S.P. / Zhang, Y. / Young, D.B. | ||||||
![]() | ![]() Title: Engineering a Change in the Metal-Ion Specificity of the Iron-Depedent Superoxide Dismutase from Mycobacterium Tuberculosis. X-Ray Structure Analysis of Site-Directed Mutants. Authors: Bunting, K.A. / Cooper, J.B. / Badasso, M.O. / Tickle, I.J. / Newton, M. / Wood, S.P. / Young, D.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86.6 KB | Display | ![]() |
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PDB format | ![]() | 65.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 423.9 KB | Display | ![]() |
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Full document | ![]() | 447.5 KB | Display | |
Data in XML | ![]() | 18.7 KB | Display | |
Data in CIF | ![]() | 22.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gn4C ![]() 1idsS C: citing same article ( S: Starting model for refinement |
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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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.9936, -0.0017, 0.1129), Vector: |
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Components
#1: Protein | Mass: 23050.844 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P17670, UniProt: P9WGE7*PLUS, superoxide dismutase #2: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 48 % |
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Crystal grow | Temperature: 277 K / pH: 7 Details: 100MM TRIS-HCL PH 7.0, 25% PEG 6000, PROTEIN CONCENTRATION = 3 MG/ML, 4 DEGREES CENTIGRADE. |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 4→99 Å / Num. obs: 5069 / % possible obs: 98.4 % / Redundancy: 9.2 % / Rmerge(I) obs: 0.163 |
Reflection shell | Rmerge(I) obs: 0.221 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1IDS Resolution: 4→20 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 4→20 Å
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Refine LS restraints |
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