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- PDB-1sxc: CRYSTAL STRUCTURE OF REDUCED BOVINE ERYTHROCYTE SUPEROXIDE DISMUT... -
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Basic information
Entry | Database: PDB / ID: 1sxc | ||||||
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Title | CRYSTAL STRUCTURE OF REDUCED BOVINE ERYTHROCYTE SUPEROXIDE DISMUTASE AT 1.9 ANGSTROMS RESOLUTION | ||||||
![]() | SUPEROXIDE DISMUTASE | ||||||
![]() | OXIDOREDUCTASE / SUPEROXIDE ACCEPTOR | ||||||
Function / homology | ![]() Platelet degranulation / Detoxification of Reactive Oxygen Species / neurofilament cytoskeleton organization / protein phosphatase 2B binding / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / regulation of protein kinase activity / retina homeostasis / negative regulation of cholesterol biosynthetic process ...Platelet degranulation / Detoxification of Reactive Oxygen Species / neurofilament cytoskeleton organization / protein phosphatase 2B binding / relaxation of vascular associated smooth muscle / response to superoxide / peripheral nervous system myelin maintenance / regulation of protein kinase activity / retina homeostasis / negative regulation of cholesterol biosynthetic process / auditory receptor cell stereocilium organization / hydrogen peroxide biosynthetic process / myeloid cell homeostasis / positive regulation of catalytic activity / muscle cell cellular homeostasis / heart contraction / superoxide metabolic process / superoxide dismutase / transmission of nerve impulse / superoxide dismutase activity / regulation of multicellular organism growth / response to axon injury / ovarian follicle development / glutathione metabolic process / embryo implantation / : / dendrite cytoplasm / removal of superoxide radicals / reactive oxygen species metabolic process / regulation of mitochondrial membrane potential / positive regulation of cytokine production / locomotory behavior / sensory perception of sound / response to hydrogen peroxide / regulation of blood pressure / protein polyubiquitination / ubiquitin-protein transferase activity / peroxisome / protein-folding chaperone binding / response to heat / cytoplasmic vesicle / spermatogenesis / proteasome-mediated ubiquitin-dependent protein catabolic process / response to ethanol / intracellular iron ion homeostasis / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / copper ion binding / neuronal cell body / protein homodimerization activity / protein-containing complex / mitochondrion / zinc ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Rypniewski, W.R. / Mangani, S. / Bruni, B. / Orioli, P. / Casati, M. / Wilson, K.S. | ||||||
![]() | ![]() Title: Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 A resolution. Authors: Rypniewski, W.R. / Mangani, S. / Bruni, B. / Orioli, P.L. / Casati, M. / Wilson, K.S. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 74 KB | Display | ![]() |
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PDB format | ![]() | 58.7 KB | Display | ![]() |
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-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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.59865, -0.79544, 0.09433), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 1 .. A 151 B 1 .. B 151 0.295 | |
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Components
#1: Protein | Mass: 15573.337 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Compound details | COMPND REDUCED WITH SODIUM DITHIONITE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57.56 % Description: THIS IS THE FINAL MODEL OBTAINED AFTER COMBINING TWO COMPLETE DATA SETS, COLLECTED FROM TWO DIFFERENT CRYSTALS. TWO OTHER MODELS OBTAINED BY REFINING AGAINST THE INDIVIDUAL DATA SETS ...Description: THIS IS THE FINAL MODEL OBTAINED AFTER COMBINING TWO COMPLETE DATA SETS, COLLECTED FROM TWO DIFFERENT CRYSTALS. TWO OTHER MODELS OBTAINED BY REFINING AGAINST THE INDIVIDUAL DATA SETS WERE USED TO ESTIMATE ATOMIC COORDINATE ERRORS FOR THIS FINAL MODEL. THIS MODEL AND THE CORRESPONDING STRUCTURE FACTORS ARE OF UNUSUALLY HIGH QUALITY FOR THIS RESOLUTION (1.9 ANGSTROMS), WITH 97% COMPLETENESS, 9.1 FOLD REDUNDANCY (TWO DATA SETS COMBINED) AND HIGH QUALITY X-RAY SOURCE (SYNCHROTRON). THE COORDINATE ERROR IN THE FINAL MODEL, ESTIMATED FROM COMPARING THE TWO INDEPENDENTLY REFINED MODELS WAS 0.08 ANGSTROMS FOR PROTEIN ATOMS, 0.07 ANGSTROMS FOR MAIN CHAIN, 0.09 ANGSTROMS FOR SIDE CHAINS. THE OTHER TWO MODELS AND THE CORRESPONDING DATA SETS HAVE BEEN DEPOSITED SEPARATELY. | |||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 60 % | |||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: microdialysis | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: CUSTOM-MADE / Detector: IMAGE PLATE / Date: Nov 16, 1992 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Num. obs: 28249 / % possible obs: 97 % / Observed criterion σ(I): 0 / Redundancy: 9.2 % / Rmerge(I) obs: 0.1 |
Reflection | *PLUS Rmerge(I) obs: 0.01 |
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Processing
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Refinement | Resolution: 1.9→10 Å / σ(F): 0 Details: GLU 119 (BOTH SUBUNITS) APPEARS ON THE ELECTRON DENSITY TO BE COVALENTLY MODIFIED. THE NATURE OF THE MODIFICATION IS UNKNOWN AND IT HAS NOT BEEN MODELLED. THE APPEARANCE OF THE ELECTRON ...Details: GLU 119 (BOTH SUBUNITS) APPEARS ON THE ELECTRON DENSITY TO BE COVALENTLY MODIFIED. THE NATURE OF THE MODIFICATION IS UNKNOWN AND IT HAS NOT BEEN MODELLED. THE APPEARANCE OF THE ELECTRON DENSITY IS CONSISTENT WITH OE1 REPLACED BY A HYDROXYLAMINE GROUP. THE MODIFICATION IS ALSO OBSERVED IN THE STRUCTURE OF NATIVE, OXIDIZED SOD. THEREFORE, IT CANNOT BE AN ARTIFACT OF THE TREATMENT WITH DITHIONITE, USED IN REDUCING THE ENZYME. THE POSITION OF THE MODIFICATION RELATIVE TO THE ACTIVE SITE SUGGESTS A ROLE IN THE REACTION MECHANISM. SEE THE PAPER CITED ON JRNL RECORDS ABOVE FOR DETAILS. RESIDUES WITH POOR ELECTRON DENSITY: LYS A 3, LYS A 9, LYS A 23, LYS A 68, LYS A 73, LYS A 89, GLU A 107, LYS A 120, LYS A 134, LYS A 151, LYS B 23, ASN B 51, GLN B 53, LYS B 73, LYS B 89, LYS B 134, LYS B 151. A NUMBER OF CLOSE CONTACTS OCCURS BETWEEN SOLVENT MOLECULES. INSPECTION OF THE ELECTRON DENSITY CONFIRMS THAT THESE SITES ARE REAL BUT PROBABLY CORRESPOND TO PARTIALLY OCCUPIED, ALTERNATIVE SOLVENT SITES. A FEW VERY CLOSE CONTACTS OCCUR BETWEEN ATOMS WITH ZERO OCCUPANCY AND SOLVENT MOLECULES.
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Displacement parameters | Biso mean: 20.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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