+Open data
-Basic information
Entry | Database: PDB / ID: 2z1x | ||||||
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Title | tRNA guanine transglycosylase E235Q mutant in complex with preQ1 | ||||||
Components | Queuine tRNA-ribosyltransferase | ||||||
Keywords | TRANSFERASE / TGT / preQ1 / E235Q mutant | ||||||
Function / homology | Function and homology information 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 | Zymomonas mobilis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.63 Å | ||||||
Authors | Tidten, N. / Stengl, B. / Heine, A. / Garcia, G.A. / Klebe, G. / Reuter, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Glutamate versus Glutamine Exchange Swaps Substrate Selectivity in tRNA-Guanine Transglycosylase: Insight into the Regulation of Substrate Selectivity by Kinetic and Crystallographic Studies Authors: Tidten, N. / Stengl, B. / Heine, A. / Garcia, G.A. / Klebe, G. / Reuter, K. | ||||||
History |
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Remark 999 | SEQUENCE THE CONFLICT INVOLVING RESIDUE 312 IS CONSISTENT WITH THE REF. 1 AND 2 IN THE UNIPROT ...SEQUENCE THE CONFLICT INVOLVING RESIDUE 312 IS CONSISTENT WITH THE REF. 1 AND 2 IN THE UNIPROT SEQUENCE DATABASE, TGT_ZYMMO. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2z1x.cif.gz | 167.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2z1x.ent.gz | 130.3 KB | Display | PDB format |
PDBx/mmJSON format | 2z1x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z1/2z1x ftp://data.pdbj.org/pub/pdb/validation_reports/z1/2z1x | HTTPS FTP |
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-Related structure data
Related structure data | 2okoC 2potC 2pwuC 2pwvC 2qiiC 2z1vC 2z1wC 1p0bS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-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
#1: Protein | Mass: 42924.719 Da / Num. of mol.: 1 / Mutation: E235Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Zymomonas mobilis (bacteria) / Gene: tgt / Plasmid: pET9d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS References: UniProt: P28720, tRNA-guanosine34 preQ1 transglycosylase | ||
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#2: Chemical | ChemComp-ZN / | ||
#3: Chemical | ChemComp-PRF / | ||
#4: Chemical | ChemComp-GOL / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.03 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 8% PEG 8000, 100mM MES pH 5.5, 1mM DTT, 10% DMSO, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54178 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Dec 4, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.63→50 Å / Num. all: 42181 / Num. obs: 42181 / % possible obs: 89.8 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 24 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1P0B Resolution: 1.63→24.1 Å / Num. parameters: 27726 / Num. restraintsaints: 35382 / Cross valid method: FREE R / Stereochemistry target values: Engh & Huber
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Refine analyze | Num. disordered residues: 9 / Occupancy sum hydrogen: 2737 / Occupancy sum non hydrogen: 3020.25 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.63→24.1 Å
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Refine LS restraints |
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