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Yorodumi- PDB-4jae: STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4jae | |||||||||
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Title | STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI complexed WITH S-CARBOXYMETHYL-COA | |||||||||
Components | Citrate synthase | |||||||||
Keywords | TRANSFERASE / CITRATE SYNTHASE / GRAM-NEGATIVE BACTERIA / ALLOSTERY / OXALOACETATE / ACETYL-COA / NADH / PROTEIN FOLDING / S-CARBOXYMETHYL-COA / ALLOSTERIC ENZYME / TRICARBOXYLIC ACID CYCLE | |||||||||
Function / homology | Function and homology information citrate synthase (unknown stereospecificity) / citrate (Si)-synthase activity / NADH binding / protein hexamerization / tricarboxylic acid cycle / identical protein binding / cytosol Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | |||||||||
Authors | Maurus, R. / Brayer, G.D. | |||||||||
Citation | Journal: Biochim.Biophys.Acta / Year: 2013 Title: Enzyme-substrate complexes of allosteric citrate synthase: Evidence for a novel intermediate in substrate binding. Authors: Duckworth, H.W. / Nguyen, N.T. / Gao, Y. / Donald, L.J. / Maurus, R. / Ayed, A. / Bruneau, B. / Brayer, G.D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4jae.cif.gz | 183.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4jae.ent.gz | 145.8 KB | Display | PDB format |
PDBx/mmJSON format | 4jae.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ja/4jae ftp://data.pdbj.org/pub/pdb/validation_reports/ja/4jae | HTTPS FTP |
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-Related structure data
Related structure data | 4jadC 4jafC 4jagC 1k3p C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 47994.785 Da / Num. of mol.: 2 / Mutation: A50T, S279G, S280K, V281K, K282E, H283N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: gltA, gluT, icdB, b0720, JW0710 / Production host: Escherichia coli (E. coli) / References: UniProt: P0ABH7, citrate (Si)-synthase #2: Chemical | ChemComp-SO4 / #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | ASPARTATE AT POSITION 10 CHAIN A AND 1010 CHAIN B IS A POST-TRANSLATIONAL MODIFICATION OF ASN THAT ...ASPARTATE AT POSITION 10 CHAIN A AND 1010 CHAIN B IS A POST-TRANSLATIO | |
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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: 4.27 Å3/Da / Density % sol: 71.2 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 2% (V/V) PEG400, 2.0-2.3 M AMMONIUM SULFATE, 0.1 M NA HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 0.97 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 28, 2008 / Details: VERTICAL FOCUSING MIRROR |
Radiation | Monochromator: SIDE SCATTERING I-BEAM BENT SINGLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. obs: 42859 / % possible obs: 98.1 % / Redundancy: 2.8 % / Rmerge(I) obs: 0.086 / Net I/σ(I): 7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1K3P 1k3p Resolution: 2.7→30 Å / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Bsol: 76.42 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48.57 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→30 Å
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Refine LS restraints |
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Xplor file |
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