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- PDB-1e1o: lysyl-tRNA Synthetase (LYSU) hexagonal form, complexed with lysine -
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Open data
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Basic information
Entry | Database: PDB / ID: 1e1o | ||||||
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Title | lysyl-tRNA Synthetase (LYSU) hexagonal form, complexed with lysine | ||||||
![]() | LYSYL-TRNA SYNTHETASE, HEAT INDUCIBLE | ||||||
![]() | LIGASE / AMINOACYL-TRNA SYNTHETASE / PROTEIN BIOSYNTHESIS | ||||||
Function / homology | ![]() RNA capping / ATP:ADP adenylyltransferase activity / lysine-tRNA ligase / lysine-tRNA ligase activity / lysyl-tRNA aminoacylation / diadenosine tetraphosphate biosynthetic process / tRNA aminoacylation for protein translation / aminoacyl-tRNA synthetase multienzyme complex / positive regulation of macrophage activation / ligase activity ...RNA capping / ATP:ADP adenylyltransferase activity / lysine-tRNA ligase / lysine-tRNA ligase activity / lysyl-tRNA aminoacylation / diadenosine tetraphosphate biosynthetic process / tRNA aminoacylation for protein translation / aminoacyl-tRNA synthetase multienzyme complex / positive regulation of macrophage activation / ligase activity / cellular response to heat / tRNA binding / magnesium ion binding / protein homodimerization activity / extracellular space / ATP binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Desogus, G. / Todone, F. / Brick, P. / Onesti, S. | ||||||
![]() | ![]() Title: Active Site of Lysyl-tRNA Synthetase: Structural Studies of the Adenylation Reaction Authors: Desogus, G. / Todone, F. / Brick, P. / Onesti, 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 | ![]() | 118 KB | Display | ![]() |
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PDB format | ![]() | 90.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.1 KB | Display | ![]() |
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Full document | ![]() | 450.2 KB | Display | |
Data in XML | ![]() | 22.7 KB | Display | |
Data in CIF | ![]() | 33.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1e1tC ![]() 1e22C ![]() 1e24C ![]() 1lylS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Details | THE PROTEIN IS AN ACTIVE DIMER. IN THE HEXAGONAL CELL THEMOLECULAR DYADE COINCIDE WITH A CRYSTALLOGRAPHIC 2-FOLDAXIS. TO GENERATE THE BIOLOGICALLY FUNCTIONAL DIMER THESYMMETRY OPERATION Y , X, -Z+1/3 NEEDS TO BE APPLIED TO THEATOMIC COORDINATES. |
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Components
#1: Protein | Mass: 57767.191 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-LYS / | ||||
#3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | Compound details | THE STRUCTURE OF E. COLI LYSYL-TRNA SYNTHETASE LYSU BOUND TO THE SUBSTRATE LYSINE HAS BEEN SOLVED ...THE STRUCTURE OF E. COLI LYSYL-TRNA SYNTHETASE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.8 Å3/Da / Density % sol: 74 % Description: STRUCTURE WAS SOLVED BY USING 1LYL COORDINATED TRANSLATED TO ACCOUNT FOR THE DIFFERENT ORIGIN OF THE RELATED HEXAGONAL CELL | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.8 Details: PROTEIN WAS CRYSTALLISED FROM 0.1M PIPES PH 6.8, 0.5 M LICL; 20% PEG 4K, 17% GLYCEROL | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 15, 1995 / Details: MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.86 Å / Relative weight: 1 |
Reflection | Resolution: 2.12→25 Å / Num. obs: 60434 / % possible obs: 99.6 % / Redundancy: 16.2 % / Rmerge(I) obs: 0.085 / Rsym value: 0.085 / Net I/σ(I): 8.8 |
Reflection shell | Resolution: 2.12→2.16 Å / Redundancy: 15.4 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 3.7 / Rsym value: 0.26 / % possible all: 99.6 |
Reflection | *PLUS Num. measured all: 977338 |
Reflection shell | *PLUS % possible obs: 99.6 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1LYL Resolution: 2.12→20 Å / Rfactor Rfree error: 0.005 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Refine analyze | Luzzati d res low obs: 20 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.12→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.12→2.22 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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