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Yorodumi- PDB-1v5v: Crystal Structure of a Component of Glycine Cleavage System: T-pr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1v5v | ||||||
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Title | Crystal Structure of a Component of Glycine Cleavage System: T-protein from Pyrococcus horikoshii OT3 at 1.5 A Resolution | ||||||
Components | aminomethyltransferase | ||||||
Keywords | TRANSFERASE / GLYCINE-CLEAVAGE SYTEM / AMINOMETHYL TRANSFERASE / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information aminomethyltransferase / aminomethyltransferase activity / glycine decarboxylation via glycine cleavage system / transaminase activity Similarity search - Function | ||||||
Biological species | Pyrococcus horikoshii (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.5 Å | ||||||
Authors | Lokanath, N.K. / Kunishima, N. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: Proteins / Year: 2004 Title: Crystal structure of a component of glycine cleavage system: T-protein from Pyrococcus horikoshii OT3 at 1.5 A resolution Authors: Lokanath, N.K. / Kuroishi, C. / Okazaki, N. / Kunishima, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1v5v.cif.gz | 179.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1v5v.ent.gz | 143.1 KB | Display | PDB format |
PDBx/mmJSON format | 1v5v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v5/1v5v ftp://data.pdbj.org/pub/pdb/validation_reports/v5/1v5v | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED FROM THE MONOMER USING SYMMETRY OPERATIONS. TWO MOLECULES IN THE ASYMMETRIC UNIT OF THE CRYSTAL FORM AS WELL AS IN SOLUTION |
-Components
#1: Protein | Mass: 46232.918 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus horikoshii (archaea) / Gene: GCS / Plasmid: PET-11A / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: O58888, aminomethyltransferase #2: Chemical | #3: Chemical | ChemComp-PEG / | #4: 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: 2.47 Å3/Da / Density % sol: 49.88 % |
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Crystal grow | Temperature: 295 K / Method: microbatch / pH: 5.9 / Details: PEG, MES, pH 5.9, MICROBATCH, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B1 / Wavelength: 2.0, 0.91971, 0.92001, 0.92540 | |||||||||||||||
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Oct 17, 2003 | |||||||||||||||
Radiation | Monochromator: GRAPHITE / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.5→30 Å / Num. all: 141103 / Num. obs: 141020 / % possible obs: 97.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.2 % / Biso Wilson estimate: 18.3 Å2 / Rmerge(I) obs: 0.049 | |||||||||||||||
Reflection shell | Resolution: 1.5→1.55 Å / % possible all: 96.8 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.5→28.5 Å / Rfactor Rfree error: 0.002 / Data cutoff high absF: 2140110.83 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 44.561 Å2 / ksol: 0.384863 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.5→28.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.59 Å / Rfactor Rfree error: 0.007 / Total num. of bins used: 6
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