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- PDB-1qdl: THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qdl | ||||||
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Title | THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS | ||||||
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![]() | LYASE / TRYPTOPHAN BIOSYNTHESIS / ANTHRANILATE SYNTHASE / GLUTAMINE AMIDOTRANSFERASE / ALLOSTERIC INTERACTION | ||||||
Function / homology | ![]() anthranilate synthase / anthranilate synthase activity / tryptophan biosynthetic process / glutamine metabolic process / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Knoechel, T. / Ivens, A. / Hester, G. / Gonzalez, A. / Bauerle, R. / Wilmanns, M. / Kirschner, K. / Jansonius, J.N. | ||||||
![]() | ![]() Title: The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications. Authors: Knochel, T. / Ivens, A. / Hester, G. / Gonzalez, A. / Bauerle, R. / Wilmanns, M. / Kirschner, K. / Jansonius, J.N. #1: ![]() Title: X-Ray Crystallographic Studies on Hyperthermostable Enzymes of the Tryptophan Biosynthesis Pathway: Three-Dimensional Structures of Indole-3-Glycerol Phosphate Synthase and Anthranilate Synthase Authors: Knoechel, T. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 132.4 KB | Display | ![]() |
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PDB format | ![]() | 104.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440.3 KB | Display | ![]() |
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Full document | ![]() | 457.2 KB | Display | |
Data in XML | ![]() | 25.6 KB | Display | |
Data in CIF | ![]() | 35.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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
#1: Protein | Mass: 47779.453 Da / Num. of mol.: 1 / Fragment: AMINODEOXYISOCHORISMATE SYNTHASE/LYASE SUBUNIT Source method: isolated from a genetically manipulated source Details: CONTAINS RESIDUES GLY-3,SER-2, HIS-1 PRIOR TO THE INITIATING METHIONINE Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 21937.258 Da / Num. of mol.: 1 / Fragment: GLUTAMINE AMIDOTRANSFERASE SUBUNIT Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | pH: 7.5 Details: SODIUM CHLORIDE, PEG 6000, POTASSIUM PHOSPHATE, pH 7.50 | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 79 % | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusionDetails: drop consists of equal volume of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||||||||
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: Jul 16, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9095 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. obs: 57136 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 9.7 % / Biso Wilson estimate: 46.7 Å2 / Rmerge(I) obs: 0.054 / Net I/σ(I): 30.49 |
Reflection shell | Resolution: 2.5→2.59 Å / Rmerge(I) obs: 0.291 / % possible all: 99.6 |
Reflection shell | *PLUS % possible obs: 99.6 % |
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Processing
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Refinement | Resolution: 2.5→30 Å / σ(F): 1 Details: A FLAT BULK-SOLVENT MODEL WAS SUPPLIED THROUGHOUT THE REFINEMENT. DIFFRACTION DATA WERE SUBJECTED TO AN OVERALL ANISOTROPIC B-FACTOR SCALING.
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Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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Refine LS restraints |
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