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Open data
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Basic information
Entry | Database: PDB / ID: 1f1a | ||||||
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Title | Crystal structure of yeast H48Q cuznsod fals mutant analog | ||||||
![]() | COPPER-ZINC SUPEROXIDE DISMUTASE | ||||||
![]() | OXIDOREDUCTASE / FALS / CuZnSOD / Lou Gehrig's Disease | ||||||
Function / homology | ![]() oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor / superoxide dismutase complex / protein maturation by copper ion transfer / negative regulation of cellular respiration / fungal-type cell wall organization / Platelet degranulation / Detoxification of Reactive Oxygen Species / intracellular zinc ion homeostasis / cellular detoxification / superoxide metabolic process ...oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor / superoxide dismutase complex / protein maturation by copper ion transfer / negative regulation of cellular respiration / fungal-type cell wall organization / Platelet degranulation / Detoxification of Reactive Oxygen Species / intracellular zinc ion homeostasis / cellular detoxification / superoxide metabolic process / superoxide dismutase / superoxide dismutase activity / intracellular copper ion homeostasis / removal of superoxide radicals / mitochondrial intermembrane space / cellular response to oxidative stress / protein stabilization / copper ion binding / positive regulation of transcription by RNA polymerase II / mitochondrion / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Hart, P.J. / Ogihara, N.L. / Liu, H. / Nersissian, A.M. / Valentine, J.S. / Eisenberg, D. | ||||||
![]() | ![]() Title: A structure-based mechanism for copper-zinc superoxide dismutase. Authors: Hart, P.J. / Balbirnie, M.M. / Ogihara, N.L. / Nersissian, A.M. / Weiss, M.S. / Valentine, J.S. / Eisenberg, 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 | ![]() | 38.6 KB | Display | ![]() |
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PDB format | ![]() | 29.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1b4lC ![]() 1b4tC ![]() 1f18C ![]() 1f1dC ![]() 1f1gC ![]() 1yazC ![]() 2jcwC 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 15864.569 Da / Num. of mol.: 1 / Mutation: H48Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Cellular location: CYTOPLASM / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-CU / |
#3: Chemical | ChemComp-ZN / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 61.66 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.7 Details: ammonium sulfate, Tris-Hcl, NaCl, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / 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→40 Å / Num. all: 97858 / Num. obs: 18709 / % possible obs: 98.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5.2 % / Biso Wilson estimate: 22.4 Å2 / Rmerge(I) obs: 0.109 / Net I/σ(I): 12.5 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.284 / Num. unique all: 1807 / % possible all: 96.7 |
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Processing
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Refinement | Resolution: 1.8→10 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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