+Open data
-Basic information
Entry | Database: PDB / ID: 8cei | ||||||
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Title | Succinyl-CoA Reductase from Clostridium kluyveri (SucD) | ||||||
Components | Succinate-semialdehyde dehydrogenase (acetylating) | ||||||
Keywords | OXIDOREDUCTASE / SSA / succinic semialdehyde / NADPH / NADP+ / SucD / ssr / succinyl-CoA / mesaconyl-CoA / mesaconyl-C1-CoA / SucD_Ck / CkSucD | ||||||
Function / homology | succinate-semialdehyde dehydrogenase (acylating) / oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, N-terminal / Aldehyde dehydrogenase, C-terminal / Aldehyde/histidinol dehydrogenase / Succinate-semialdehyde dehydrogenase (acetylating) Function and homology information | ||||||
Biological species | Clostridium kluyveri (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Pfister, P. / Diehl, C. / Erb, T.J. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Biochemistry / Year: 2023 Title: Enhancing the Substrate Specificity of Clostridium Succinyl-CoA Reductase for Synthetic Biology and Biocatalysis. Authors: Pfister, P. / Diehl, C. / Hammarlund, E. / Carrillo, M. / Erb, T.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8cei.cif.gz | 692.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8cei.ent.gz | 575.1 KB | Display | PDB format |
PDBx/mmJSON format | 8cei.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ce/8cei ftp://data.pdbj.org/pub/pdb/validation_reports/ce/8cei | HTTPS FTP |
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-Related structure data
Related structure data | 8cejC 8cekC 3k9dS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 49029.910 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium kluyveri (bacteria) / Gene: sucD, CKL_3015 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P38947, succinate-semialdehyde dehydrogenase (acylating) #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.86 % |
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Crystal grow | Temperature: 288.15 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 25 % w/v Pentaerythritol Propoxylate (5/4 PO/OH) 100 mM MES; pH 6.5 50 mM Magnesium chloride PH range: 6.5-7.8 |
-Data collection
Diffraction | Mean temperature: 80 K / Ambient temp details: cryostream / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 0.9762 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 30, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9762 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→39.47 Å / Num. obs: 197254 / % possible obs: 99.2 % / Redundancy: 4.4 % / CC1/2: 0.995 / Rpim(I) all: 0.054 / Rrim(I) all: 0.116 / Net I/σ(I): 7.3 |
Reflection shell | Resolution: 2.2→2.32 Å / % possible obs: 96 % / Redundancy: 4.4 % / Num. measured all: 62718 / Num. unique obs: 14359 / CC1/2: 0.945 / Rpim(I) all: 0.22 / Rrim(I) all: 0.468 / Net I/σ(I) obs: 2.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3K9D Resolution: 2.2→39.47 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.41 / Phase error: 33.66 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→39.47 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 1.1918 Å / Origin y: -0.932 Å / Origin z: 89.664 Å
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Refinement TLS group | Selection details: all |