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- PDB-8j29: Structures of the C-terminal subenzyme of the malonyl-CoA reducta... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8j29 | ||||||
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Title | Structures of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus | ||||||
![]() | Short-chain dehydrogenase/reductase SDR | ||||||
![]() | OXIDOREDUCTASE / 3-hydroxypropionate(3-HP) / malonyl-CoA reductase / CO2 fixation / short-chain dehydrogenase/reductase (SDR) / Chloroflexus aurantiacus | ||||||
Function / homology | fatty acid elongation / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / short chain dehydrogenase / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding domain superfamily / nucleotide binding / metal ion binding / L(+)-TARTARIC ACID / Short-chain dehydrogenase/reductase SDR![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ma, Q. / Liu, C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structures of the C-terminal subenzyme of the malonyl-CoA reductase from Chloroflexus aurantiacus Authors: Ma, Q. / Liu, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 265.9 KB | Display | ![]() |
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PDB format | ![]() | 211.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 445.2 KB | Display | ![]() |
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Full document | ![]() | 446.6 KB | Display | |
Data in XML | ![]() | 26 KB | Display | |
Data in CIF | ![]() | 39.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8j2aC ![]() 8j2bC ![]() 8j2cC ![]() 8j2dC ![]() 8j2eC C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 73651.859 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: Caur_2614 / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-TLA / |
#3: Chemical | ChemComp-GOL / |
#4: Water | ChemComp-HOH / |
Has ligand of interest | N |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.87 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: The protein was crystallized in drops containing 1.5 ul protein solution (10 mg/ml) and 1.5 ul reservoir solution (900 mM ammonium tartrate pH 6.0) |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 17, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97852 Å / Relative weight: 1 |
Reflection | Resolution: 1.877→72.902 Å / Num. obs: 68842 / % possible obs: 97.7 % / Redundancy: 7 % / CC1/2: 1 / Rpim(I) all: 0.021 / Rrim(I) all: 0.056 / Rsym value: 0.051 / Net I/σ(I): 21.9 |
Reflection shell | Resolution: 1.877→1.883 Å / Redundancy: 7.1 % / Mean I/σ(I) obs: 2.3 / Num. unique obs: 657 / CC1/2: 0.877 / Rpim(I) all: 0.282 / Rrim(I) all: 0.76 / Rsym value: 0.705 / % possible all: 97.9 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 38.69 Å2
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Refine analyze | Luzzati coordinate error obs: 0.23 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 1.88→27.53 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.88→1.93 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: -0.3265 Å / Origin y: 71.5753 Å / Origin z: 57.9217 Å
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Refinement TLS group | Selection details: { A|561 - A|1219 } |