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- PDB-2du7: Crystal structure of Methanococcus jannacshii O-phosphoseryl-tRNA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2du7 | ||||||
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Title | Crystal structure of Methanococcus jannacshii O-phosphoseryl-tRNA synthetase | ||||||
![]() | O-phosphoseryl-tRNA synthetase | ||||||
![]() | LIGASE / alpha4 tetramer / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | ![]() O-phospho-L-serine-tRNA ligase / phosphoserine-tRNA(Cys) ligase activity / phenylalanine-tRNA ligase activity / phenylalanyl-tRNA aminoacylation / tRNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fukunaga, R. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea. Authors: Fukunaga, R. / Yokoyama, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 388.5 KB | Display | ![]() |
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PDB format | ![]() | 322.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 472.6 KB | Display | ![]() |
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Full document | ![]() | 597.3 KB | Display | |
Data in XML | ![]() | 87.9 KB | Display | |
Data in CIF | ![]() | 114.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2du3SC ![]() 2du4C ![]() 2du5C ![]() 2du6C S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 63527.578 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pET26b / Production host: ![]() ![]() References: UniProt: Q59054, Ligases; Forming carbon-oxygen bonds; Ligases forming aminoacyl-tRNA and related compounds |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.64 Å3/Da / Density % sol: 66.2 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.7 Details: 11.25% PEG 4000, 75mM Na-citrate, 75mM ADA-NaOH buffer (pH 6.7), VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 30, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.6→20 Å / Num. all: 43084 / Num. obs: 42030 / % possible obs: 97.6 % / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 3.6→3.73 Å / % possible all: 94.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2DU3 Resolution: 3.6→19.79 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 7089748.71 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 32.9985 Å2 / ksol: 0.194656 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 129.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.6→19.79 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.6→3.82 Å / Rfactor Rfree error: 0.017 / Total num. of bins used: 6
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Xplor file |
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