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Open data
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Basic information
Entry | Database: PDB / ID: 1yge | ||||||
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Title | LIPOXYGENASE-1 (SOYBEAN) AT 100K | ||||||
![]() | LIPOXYGENASE-1 | ||||||
![]() | DIOXYGENASE / LIPOXYGENASE / METALLOPROTEIN / FATTY ACIDS | ||||||
Function / homology | ![]() linolenate 9R-lipoxygenase activity / linoleate 13S-lipoxygenase / linoleate 13S-lipoxygenase activity / oxylipin biosynthetic process / lipid oxidation / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / fatty acid oxidation / fatty acid biosynthetic process / iron ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Minor, W. / Steczko, J. / Stec, B. / Otwinowski, Z. / Bolin, J.T. / Walter, R. / Axelrod, B. | ||||||
![]() | ![]() Title: Crystal structure of soybean lipoxygenase L-1 at 1.4 A resolution. Authors: Minor, W. / Steczko, J. / Stec, B. / Otwinowski, Z. / Bolin, J.T. / Walter, R. / Axelrod, B. #1: ![]() Title: Position 713 is Critical for Catalysis But not Iron Binding in Soybean Lipoxygenase Authors: Kramer, J.A. / Johnson, K.R. / Dunham, W.R. / Sands, R.H. / Funk Junior, M.O. #2: ![]() Title: The Structure and Function of Lipoxygenase Authors: Nelson, M.J. / Seitz, S.P. #3: ![]() Title: Structural Characterization of Alkyl and Peroxyl Radicals in Solutions of Purple Lipoxygenase Authors: Nelson, M.J. / Cowling, R.A. / Seitz, S.P. #4: ![]() Title: X-Ray Spectroscopy of the Iron Site in Soybean Lipoxygenase-1: Changes in Coordination Upon Oxidation or Addition of Methanol Authors: Scarrow, R.C. / Trimitsis, M.G. / Buck, C.P. / Grove, G.N. / Cowling, R.A. / Nelson, M.J. #5: ![]() Title: The Three-Dimensional Structure of an Arachidonic Acid 15-Lipoxygenase Authors: Boyington, J.C. / Gaffney, B.J. / Amzel, L.M. #6: ![]() Title: Crystallographic Determination of the Active Site Iron and its Ligands in Soybean Lipoxygenase L-1 Authors: Minor, W. / Steczko, J. / Bolin, J.T. / Otwinowski, Z. / Axelrod, B. #7: ![]() Title: Conserved Histidine Residues in Soybean Lipoxygenase: Functional Consequences of Their Replacement Authors: Steczko, J. / Donoho, G.P. / Clemens, J.C. / Dixon, J.E. / Axelrod, B. #8: ![]() Title: Spectroscopic Studies of the Non-Heme Ferric Active Site in Soybean Lipoxygenase: Magnetic Circular Dichroism as a Probe of Electronic and Geometric Structure. Ligand-Field Origin of Zero-Field Authors: Zhang, Y. / Gebhard, M.S. / Solomon, E.I. #9: ![]() Title: Crystallization and Preliminary X-Ray Investigation of Lipoxygenase 1 from Soybeans Authors: Steczko, J. / Muchmore, C.R. / Smith, J.L. / Axelrod, B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 213 KB | Display | ![]() |
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PDB format | ![]() | 165.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 371.5 KB | Display | ![]() |
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Full document | ![]() | 377.2 KB | Display | |
Data in XML | ![]() | 17 KB | Display | |
Data in CIF | ![]() | 34.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 94480.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-FE / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 48 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 5.6 / Method: vapor diffusion, sitting drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MAC Science DIP-2000 / Detector: IMAGE PLATE / Date: Apr 1, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 161029 / % possible obs: 96 % / Observed criterion σ(I): -3 / Redundancy: 3 % / Rmerge(I) obs: 0.067 |
Reflection | *PLUS Highest resolution: 1.4 Å / Lowest resolution: 40 Å / Num. all: 169235 |
Reflection shell | *PLUS Highest resolution: 1.4 Å / Lowest resolution: 1.42 Å / % possible obs: 92 % |
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Processing
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Refinement | Resolution: 1.4→10 Å / σ(F): 2 Details: THE ELECTRON DENSITY FOR RESIDUES 1 - 6 IS WEAK AND FRAGMENTED SUGGESTING THAT THIS IS A MOBILE SEGMENT. FOR RESIDUES 22 - 30, WHICH FORM PART OF AN EXTENDED LOOP, THE DENSITY INDICATES THE ...Details: THE ELECTRON DENSITY FOR RESIDUES 1 - 6 IS WEAK AND FRAGMENTED SUGGESTING THAT THIS IS A MOBILE SEGMENT. FOR RESIDUES 22 - 30, WHICH FORM PART OF AN EXTENDED LOOP, THE DENSITY INDICATES THE COURSE OF THE POLYPEPTIDE AND THE LOCATION OF THE SIDE CHAINS, BUT IS NOT FULLY CONTINUOUS. TWO ADDITIONAL LOOPS, COMPRISING RESIDUES 70 - 73 AND 116 - 120, ARE REPRESENTED BY CONTINUOUS, BUT LESS THAN DEFINITE DENSITY. ALL FOUR SEGMENTS ARE INCLUDED IN THE CURRENT MODEL.
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Displacement parameters | Biso mean: 17.2 Å2 | |||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.2 Å | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.4→10 Å
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Software | *PLUS Name: ![]() | |||||||||||||||
Refinement | *PLUS | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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