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Yorodumi- PDB-1uc9: Crystal structure of a lysine biosynthesis enzyme, Lysx, from the... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1uc9 | ||||||
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Title | Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8 | ||||||
Components | lysine biosynthesis enzyme | ||||||
Keywords | BIOSYNTHETIC PROTEIN / LYSINE BIOSYNTHESIS / ALPHA-AMINOADIPATE PATHWAY / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | Function and homology information [amino-group carrier protein]-L-2-aminoadipate ligase / N-acetyl-L-aspartate-L-glutamate ligase activity / ribosomal S6-glutamic acid ligase activity / lysine biosynthetic process via aminoadipic acid / protein modification process => GO:0036211 / ligase activity / SOS response / protein modification process / ATP binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.38 Å | ||||||
Authors | Sakai, H. / Vassylyeva, M.N. / Matsuura, T. / Sekine, S. / Nishiyama, M. / Terada, T. / Shirouzu, M. / Kuramitsu, S. / Vassylyev, D.G. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: Crystal Structure of a Lysine Biosynthesis Enzyme, LysX, from Thermus thermophilus HB8 Authors: Sakai, H. / Vassylyeva, M.N. / Matsuura, T. / Sekine, S. / Gotoh, K. / Nishiyama, M. / Terada, T. / Shirouzu, M. / Kuramitsu, S. / Vassylyev, D.G. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uc9.cif.gz | 110.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uc9.ent.gz | 85 KB | Display | PDB format |
PDBx/mmJSON format | 1uc9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uc/1uc9 ftp://data.pdbj.org/pub/pdb/validation_reports/uc/1uc9 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is assumed to be a dimer in the crystallographic assymetric unit. |
-Components
#1: Protein | Mass: 30425.240 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Plasmid: pET26B / Production host: Escherichia coli (E. coli) / References: UniProt: Q84BR0, UniProt: Q5SH23*PLUS #2: Chemical | #3: 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: 2.38 Å3/Da / Density % sol: 48.38 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: PEG4000, Na acetate, ammonium acetate, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.0K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / Method: vapor diffusion, sitting dropDetails: Vassylyeva, M.N., (2003) Acta Crystallogr., D59, 1651. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44B2 / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 4, 2002 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→50 Å / Num. all: 22847 / Num. obs: 22847 / % possible obs: 98.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.3 % / Biso Wilson estimate: 36.6 Å2 / Rmerge(I) obs: 0.036 / Net I/σ(I): 21.9 |
Reflection shell | Resolution: 2.38→2.47 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.234 / Mean I/σ(I) obs: 5.5 / % possible all: 94.4 |
Reflection | *PLUS |
Reflection shell | *PLUS % possible obs: 94.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.38→49.8 Å / Rfactor Rfree error: 0.009 / Data cutoff high rms absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 47.2958 Å2 / ksol: 0.361808 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 48.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.38→49.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.38→2.53 Å / Rfactor Rfree error: 0.028 / Total num. of bins used: 6
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Refinement | *PLUS Rfactor Rfree: 0.28 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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