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Yorodumi- PDB-1dl3: CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSP... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dl3 | ||||||
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Title | CRYSTAL STRUCTURE OF MUTUALLY GENERATED MONOMERS OF DIMERIC PHOSPHORIBOSYLANTRANILATE ISOMERASE FROM THERMOTOGA MARITIMA | ||||||
Components | PROTEIN (PHOSPHORIBOSYLANTRANILATE ISOMERASE) | ||||||
Keywords | ISOMERASE / OLIGOMERISATION / THERMOSTABILITY / THERMOTOGA MARITIMA / PROTEIN ENGINEERING / DIMER EVOLUTION | ||||||
Function / homology | Function and homology information phosphoribosylanthranilate isomerase / phosphoribosylanthranilate isomerase activity / tryptophan biosynthetic process Similarity search - Function | ||||||
Biological species | Thermotoga maritima (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.7 Å | ||||||
Authors | Thoma, R. / Hennig, M. / Sterner, R. / Kirschner, K. | ||||||
Citation | Journal: Structure Fold.Des. / Year: 2000 Title: Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Authors: Thoma, R. / Hennig, M. / Sterner, R. / Kirschner, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dl3.cif.gz | 87.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dl3.ent.gz | 67.5 KB | Display | PDB format |
PDBx/mmJSON format | 1dl3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dl/1dl3 ftp://data.pdbj.org/pub/pdb/validation_reports/dl/1dl3 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 22973.348 Da / Num. of mol.: 2 / Mutation: A25Y,F55E,I101W Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermotoga maritima (bacteria) / Plasmid: PET11C-TTRPF / Production host: Escherichia coli (E. coli) / Keywords: ENGINEERED MUTATION References: UniProt: Q56320, phosphoribosylanthranilate isomerase #2: Chemical | #3: 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: 2.16 Å3/Da / Density % sol: 43.07 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: 1 MM EDTA 0.5 MM DTT 0.1 M HEPES/NAOH 16.7 MG/ML PROTEIN 0.75 M POTASSIUM DIHYDROGEN PHOSPHATE 0.75 M SODIUM DIHYDROGEN PHOSPHATE, pH 7.5, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: ENRAF-NONIUS FR571 / Wavelength: 1.54 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 18, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→20 Å / Num. all: 51809 / Num. obs: 11375 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 31 Å2 / Rmerge(I) obs: 0.076 / Net I/σ(I): 8.2 |
Reflection | *PLUS Num. measured all: 51809 |
Reflection shell | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 2.8 Å / % possible obs: 98.7 % / Rmerge(I) obs: 0.317 |
-Processing
Software |
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Refinement | Resolution: 2.7→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 20 Å / σ(F): 0 / Rfactor obs: 0.175 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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