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- PDB-5v2z: Ethylene forming enzyme in complex with manganese, 2-oxoadipic ac... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5v2z | ||||||
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Title | Ethylene forming enzyme in complex with manganese, 2-oxoadipic acid and L-arginine | ||||||
![]() | 2-oxoglutarate-dependent ethylene/succinate-forming enzyme | ||||||
![]() | OXIDOREDUCTASE / 2-oxoadipic acid / alpha-Ketoadipic acid / 2-oxohexanedioic acid / 2-oxoadipate / ethylene biosynthesis | ||||||
Function / homology | ![]() 2-oxoglutarate dioxygenase (ethene-forming) / 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming) / 2-oxoglutarate oxygenase/decarboxylase (ethylene-forming) activity / ethylene biosynthetic process / 2-oxoglutarate-dependent dioxygenase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Fellner, M. / Martinez, S. / Hu, J. / Hausinger, R.P. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structures and Mechanisms of the Non-Heme Fe(II)- and 2-Oxoglutarate-Dependent Ethylene-Forming Enzyme: Substrate Binding Creates a Twist. Authors: Martinez, S. / Fellner, M. / Herr, C.Q. / Ritchie, A. / Hu, J. / Hausinger, R.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 227.2 KB | Display | ![]() |
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PDB format | ![]() | 183.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 458.3 KB | Display | ![]() |
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Full document | ![]() | 459.3 KB | Display | |
Data in XML | ![]() | 19.2 KB | Display | |
Data in CIF | ![]() | 30.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5v2tSC ![]() 5v2uC ![]() 5v2vC ![]() 5v2xC ![]() 5v2yC ![]() 5v31C ![]() 5v32C ![]() 5v34C ![]() 5vkaC ![]() 5vkbC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 39716.762 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: efe / Plasmid: pET28 / Production host: ![]() ![]() References: UniProt: P32021, 2-oxoglutarate dioxygenase (ethene-forming), EC: 1.14.11.34 |
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#2: Chemical | ChemComp-MN / |
#3: Chemical | ChemComp-OOG / |
#4: Chemical | ChemComp-ARG / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.74 % / Mosaicity: 0.27 ° |
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Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 0.5 ul 64 mg/ml EFE (+1 mM manganese chloride, 25 mM HEPES pH 8.0, 1 mM TCEP, +3 mM L-arginine, +3 mM 2-oxoadipic acid) was mixed with 0.2 ul reservoir solution. The sitting drop reservoir ...Details: 0.5 ul 64 mg/ml EFE (+1 mM manganese chloride, 25 mM HEPES pH 8.0, 1 mM TCEP, +3 mM L-arginine, +3 mM 2-oxoadipic acid) was mixed with 0.2 ul reservoir solution. The sitting drop reservoir of 200 ul contained 25% PEG 3350, 100 mM Bis-Tris, pH 6.5, 200 mM NaCl. The crystal was soaked for about a minute in 25% w/v Polyethylene glycol 400, 75% reservoir solution before freezing it. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Feb 11, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1272 Å / Relative weight: 1 |
Reflection | Resolution: 1.23→48.45 Å / Num. obs: 100282 / % possible obs: 98.7 % / Redundancy: 10.1 % / Biso Wilson estimate: 9.78 Å2 / Rmerge(I) obs: 0.083 / Net I/σ(I): 14.6 |
Reflection shell | Resolution: 1.23→1.25 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.623 / Num. unique all: 4164 / CC1/2: 0.816 / Rpim(I) all: 0.311 / Rrim(I) all: 0.699 / % possible all: 84.1 |
-Phasing
Phasing | Method: ![]() | |||||||||
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Phasing MR |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5V2T Resolution: 1.23→41.69 Å / SU ML: 0.1 / Cross valid method: FREE R-VALUE / σ(F): 1.91 / Phase error: 14.6
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.68 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.23→41.69 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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