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- PDB-1isa: 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: 1isa | ||||||
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Title | STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS | ||||||
![]() | IRON(II) SUPEROXIDE DISMUTASE | ||||||
![]() | OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) | ||||||
Function / homology | ![]() response to superoxide / superoxide metabolic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() 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: ![]() 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. #2: ![]() Title: Iron Superoxide Dismutase: Nucleotide Sequence of the Gene from Escherichia Coli K12 and Correlation with Crystal Structures Authors: Carlioz, A. / Ludwig, M.L. / Stallings, W.C. / Fee, J.A. / Steinman, H.M. / Touati, D. | ||||||
History |
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Remark 650 | HELIX ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE ALGORITHM OF KABSCH AND SANDER. ...HELIX ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE ALGORITHM OF KABSCH AND SANDER. EXCEPTIONS: THE FIRST HELIX HAS A KINK NEAR RESIDUE 28; SUCCESSIVE 3/10 TURNS ARE GIVEN PRIORITY OVER SHORT HELICES. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 90.7 KB | Display | ![]() |
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PDB format | ![]() | 69.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-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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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 16 / 2: CIS PROLINE - PRO B 16 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.1465, -0.9542, 0.2607), 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: 21154.486 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P09157, UniProt: P0AGD3*PLUS, ![]() #2: Chemical | #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.45 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, hanging dropDetails: taken from Stallings, W.C.(1983). Proc. Natl. Acad. Sci. U.S.A., 80, 3884-3888. | ||||||||||||||||||||||||||||||||||||
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: 40 Å / Num. obs: 37923 / % possible obs: 92 % / Redundancy: 4.2 % / Rmerge(I) obs: 0.0591 / Rmerge F obs: 0.1 |
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Processing
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Refinement | Resolution: 1.8→40 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.8→40 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.188 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.739 |