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Yorodumi- PDB-1ba9: THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE,... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ba9 | ||||||
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Title | THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES | ||||||
Components | SUPEROXIDE DISMUTASE | ||||||
Keywords | OXIDOREDUCTASE / SUPEROXIDE DISMUTASE / COPPER-ZINC ENZYME / DISMUTATION OF UPEROXIDE RADICALS TO MOLECULAR OXYGEN AND HYDROGEN PEROXIDE | ||||||
Function / homology | Function and homology information action potential initiation / neurofilament cytoskeleton organization / anterograde axonal transport / retrograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / protein phosphatase 2B binding / regulation of organ growth / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance ...action potential initiation / neurofilament cytoskeleton organization / anterograde axonal transport / retrograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / protein phosphatase 2B binding / regulation of organ growth / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / regulation of T cell differentiation in thymus / superoxide anion generation / retina homeostasis / negative regulation of cholesterol biosynthetic process / hydrogen peroxide biosynthetic process / auditory receptor cell stereocilium organization / regulation of protein kinase activity / myeloid cell homeostasis / muscle cell cellular homeostasis / regulation of GTPase activity / superoxide metabolic process / heart contraction / positive regulation of catalytic activity / superoxide dismutase / Detoxification of Reactive Oxygen Species / transmission of nerve impulse / negative regulation of reproductive process / negative regulation of developmental process / superoxide dismutase activity / neuronal action potential / regulation of multicellular organism growth / response to axon injury / ectopic germ cell programmed cell death / glutathione metabolic process / positive regulation of phagocytosis / ovarian follicle development / axon cytoplasm / embryo implantation / reactive oxygen species metabolic process / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / dendrite cytoplasm / removal of superoxide radicals / positive regulation of superoxide anion generation / regulation of mitochondrial membrane potential / thymus development / locomotory behavior / placenta development / response to organic substance / determination of adult lifespan / positive regulation of cytokine production / sensory perception of sound / response to hydrogen peroxide / mitochondrial intermembrane space / small GTPase binding / regulation of blood pressure / negative regulation of inflammatory response / peroxisome / Platelet degranulation / gene expression / response to heat / protein-folding chaperone binding / cytoplasmic vesicle / spermatogenesis / response to ethanol / intracellular iron ion homeostasis / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / mitochondrial matrix / response to xenobiotic stimulus / positive regulation of apoptotic process / copper ion binding / neuronal cell body / apoptotic process / protein-containing complex / mitochondrion / extracellular space / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / TORTION ANGLES DYNAMIC (DYANA) | ||||||
Authors | Banci, L. / Benedetto, M. / Bertini, I. / Del Conte, R. / Piccioli, M. / Viezzoli, M.S. | ||||||
Citation | Journal: Biochemistry / Year: 1998 Title: Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?. Authors: Banci, L. / Benedetto, M. / Bertini, I. / Del Conte, R. / Piccioli, M. / Viezzoli, M.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ba9.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1ba9.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 1ba9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ba/1ba9 ftp://data.pdbj.org/pub/pdb/validation_reports/ba/1ba9 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 15832.447 Da / Num. of mol.: 1 / Mutation: C6A, F50E, G51E, C111S, E133Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HSOD / Cellular location (production host): PERIPLASM / Gene (production host): HSOD / Production host: Escherichia coli (E. coli) / Strain (production host): TOPP 1 (STRATAGENE) / References: UniProt: P00441, superoxide dismutase |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-CU1 / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N LABELED SOD. |
-Sample preparation
Details | Contents: H2O AND D2O |
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Sample conditions | pH: 5 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
Software | Name: AMBER / Classification: refinement | ||||||||||||||||
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NMR software |
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Refinement | Method: TORTION ANGLES DYNAMIC (DYANA) / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 36 / Conformers submitted total number: 36 |