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- PDB-4q4o: tRNA-Guanine Transglycosylase (TGT) in Complex with 6-Amino-2-{[2... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4q4o | ||||||
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Title | tRNA-Guanine Transglycosylase (TGT) in Complex with 6-Amino-2-{[2-(piperidin-1-yl)ethyl]amino}-1H,7H,8H-imidazo[4,5-g]quinazolin-8-one | ||||||
![]() | Queuine tRNA-ribosyltransferase | ||||||
![]() | Transferase/transferase inhibitor / Transferase / Guanine Exchange Enzyme / preQ1 / tRNA / Transferase-transferase inhibitor complex | ||||||
Function / homology | ![]() tRNA-guanosine34 preQ1 transglycosylase / tRNA wobble guanine modification / tRNA-guanosine(34) queuine transglycosylase activity / tRNA-guanine transglycosylation / queuosine biosynthetic process / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Neeb, M. / Heine, A. / Klebe, G. | ||||||
![]() | ![]() Title: Beyond Affinity: Enthalpy-Entropy Factorization Unravels Complexity of a Flat Structure-Activity Relationship for Inhibition of a tRNA-Modifying Enzyme. Authors: Neeb, M. / Betz, M. / Heine, A. / Barandun, L.J. / Hohn, C. / Diederich, F. / Klebe, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 177.6 KB | Display | ![]() |
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PDB format | ![]() | 138.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4q4pC ![]() 4q4qC ![]() 4q4rC ![]() 4q4sC ![]() 1pudS C: citing same article ( S: Starting model for refinement |
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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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Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 42925.703 Da / Num. of mol.: 1 / Fragment: Guanine Insertion Enzyme Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 31821 / ZM4 / CP4 / Gene: tgt, ZMO0363 / Plasmid: pET9d-ZM4 / Production host: ![]() ![]() References: UniProt: P28720, tRNA-guanosine34 preQ1 transglycosylase |
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-Non-polymers , 6 types, 395 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/2YM.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/2YM.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-ZN / | ||||||
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#3: Chemical | ChemComp-DMS / | ||||||
#4: Chemical | #5: Chemical | ChemComp-CL / | #6: Chemical | ChemComp-2YM / | #7: Water | ChemComp-HOH / | |
-Details
Sequence details | AUTHORS HAVE INDICATED THE CORRECT RESIDUE AT THE POSITION IS LYS. E.G. REUTER K. K. H., FICNER R.; ...AUTHORS HAVE INDICATED THE CORRECT RESIDUE AT THE POSITION IS LYS. E.G. REUTER K. K. H., FICNER R.; J. BACTERIOL. 177:5284-5288(1995). |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.51 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 100 mM MES, 10% DMSO, 13% PEG 8000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Apr 4, 2013 / Details: Mirror |
Radiation | Monochromator: Double Crystal Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 1.35→30 Å / Num. obs: 87189 / % possible obs: 98.8 % / Redundancy: 2.1 % / Biso Wilson estimate: 14.9 Å2 / Rsym value: 0.046 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 1.35→1.37 Å / Redundancy: 2 % / Mean I/σ(I) obs: 2 / Num. unique all: 4254 / Rsym value: 0.388 / % possible all: 98.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1PUD Resolution: 1.35→27.133 Å / SU ML: 0.13 / Cross valid method: R-free / σ(F): 1.34 / Phase error: 16.02 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.35→27.133 Å
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Refine LS restraints |
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LS refinement shell |
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