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- PDB-1mng: STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARIS... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mng | ||||||
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Title | STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS | ||||||
![]() | MANGANESE SUPEROXIDE DISMUTASE | ||||||
![]() | OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) | ||||||
Function / homology | ![]() superoxide dismutase / superoxide dismutase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Lah, M.S. / Dixon, M. / Pattridge, K.A. / Stallings, W.C. / Fee, J.A. / Ludwig, M.L. | ||||||
![]() | ![]() Title: Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Authors: Lah, M.S. / Dixon, M.M. / Pattridge, K.A. / Stallings, W.C. / Fee, J.A. / Ludwig, M.L. #1: ![]() Title: Manganese Superoxide Dismutase from Thermus Thermophilus. A Structural Model Refined at 1.8 Angstroms Resolution Authors: Ludwig, M.L. / Metzger, A.L. / Pattridge, K.A. / Stallings, W.C. #2: ![]() Year: 1992 Title: Iron and Manganese Superoxide Dismutases: Catalytic Inferences from the Structures Authors: Stallings, W.C. / Bull, C. / Fee, J.A. / Lah, M.S. / Ludwig, M.L. #3: ![]() Title: Structure-Function Relationships in Fe-and Mn-Superoxide Dismutases Authors: Stallings, W.C. / Metzger, A.L. / Pattridge, K.A. / Fee, J.A. / Ludwig, M.L. #4: ![]() Title: The Structure of Manganese Superoxide Dismutase from Thermus Thermophilus at 2.4 Angstroms Resolution Authors: Stallings, W.C. / Pattridge, K.A. / Strong, R.K. / Ludwig, M.L. #5: ![]() Title: Manganese and Iron Superoxide Dismutases are Structural Homologs Authors: Stallings, W.C. / Pattridge, K.A. / Strong, R.K. / Ludwig, M.L. | ||||||
History |
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Remark 650 | HELIX ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE ALGORITHM OF KABSCH AND SANDER, WITH THE ...HELIX ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE ALGORITHM OF KABSCH AND SANDER, WITH THE FOLLOWING EXCEPTIONS: HELICES START WITH THE FIRST RESIDUE HAVING A HELICAL HYDROGEN BOND; SUCCESSIVE 3/10 TURNS ARE GIVEN PRIORITY OVER SHORT 3/10 HELICES. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 99 KB | Display | ![]() |
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PDB format | ![]() | 77.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 376.7 KB | Display | ![]() |
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Full document | ![]() | 379.8 KB | Display | |
Data in XML | ![]() | 9.5 KB | Display | |
Data in CIF | ![]() | 15.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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Atom site foot note | 1: CIS PROLINE - PRO A 3 / 2: CIS PROLINE - PRO A 18 / 3: CIS PROLINE - PRO B 3 / 4: CIS PROLINE - PRO B 18 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.0569, -0.94416, 0.32454), Vector: Details | THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*. | |
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Components
#1: Protein | Mass: 23129.295 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.24 Å3/Da / Density % sol: 61.99 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 20 Å / Num. obs: 52673 / Redundancy: 6.5 % / Rmerge(I) obs: 0.077 |
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Processing
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Refinement | Resolution: 1.8→20 Å / σ(F): 0 Details: FOR ATOMS THAT ARE PRESENTED IN ALTERNATE CONFORMATIONS, THE ALTERNATE LOCATION INDICATOR *L* REPRESENTS THOSE ATOMS IN THE CONFORMATION WITH AZIDE LIGANDED AND *U* REPRESENTS THOSE ATOMS IN ...Details: FOR ATOMS THAT ARE PRESENTED IN ALTERNATE CONFORMATIONS, THE ALTERNATE LOCATION INDICATOR *L* REPRESENTS THOSE ATOMS IN THE CONFORMATION WITH AZIDE LIGANDED AND *U* REPRESENTS THOSE ATOMS IN THE CONFORMATION WITHOUT AZIDE LIGANDED.
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |