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Yorodumi- PDB-1juk: INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1juk | ||||||
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Title | INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS IN A TRIGONAL CRYSTAL FORM | ||||||
Components | INDOLE-3-GLYCEROL PHOSPHATE SYNTHASE | ||||||
Keywords | LYASE / THERMOPHILE / TIM-BARREL / TRYPTOPHAN BIOSYNTHESIS | ||||||
Function / homology | Function and homology information indole-3-glycerol-phosphate synthase / indole-3-glycerol-phosphate synthase activity / phosphoribosylanthranilate isomerase activity / tryptophan biosynthetic process Similarity search - Function | ||||||
Biological species | Sulfolobus solfataricus (archaea) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Knoechel, T.R. / Hennig, M. / Merz, A. / Darimont, B. / Kirschner, K. / Jansonius, J.N. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: effects of ionic strength. Authors: Knochel, T.R. / Hennig, M. / Merz, A. / Darimont, B. / Kirschner, K. / Jansonius, J.N. #1: Journal: Structure / Year: 1995 Title: 2.0 A Structure of Indole-3-Glycerol Phosphate Synthase from the Hyperthermophile Sulfolobus Solfataricus: Possible Determinants of Protein Stability Authors: Hennig, M. / Darimont, B. / Sterner, R. / Kirschner, K. / Jansonius, J.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1juk.cif.gz | 59.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1juk.ent.gz | 46.6 KB | Display | PDB format |
PDBx/mmJSON format | 1juk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ju/1juk ftp://data.pdbj.org/pub/pdb/validation_reports/ju/1juk | HTTPS FTP |
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-Related structure data
Related structure data | 1julC 1igsS 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
#1: Protein | Mass: 28626.102 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: TRIGONAL CRYSTAL FORM / Source: (gene. exp.) Sulfolobus solfataricus (archaea) / Strain: M4 / Gene: TRPC / Plasmid: PDS SS-1 / Gene (production host): TRPC / Production host: Escherichia coli (E. coli) References: UniProt: Q06121, indole-3-glycerol-phosphate synthase |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 58 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.0 | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 10, 1994 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→12.4 Å / Num. obs: 9631 / % possible obs: 95.5 % / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Rmerge(I) obs: 0.093 / Net I/σ(I): 7.1 |
Reflection shell | Resolution: 2.5→2.56 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.295 / Mean I/σ(I) obs: 2.5 / % possible all: 50.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1IGS Resolution: 2.5→10 Å / σ(F): 0
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Displacement parameters | Biso mean: 18.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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