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Yorodumi- PDB-1lbl: Crystal structure of indole-3-glycerol phosphate synthase (IGPS) ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lbl | ||||||
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Title | Crystal structure of indole-3-glycerol phosphate synthase (IGPS) in complex with 1-(o-carboxyphenylamino)-1-deoxyribulose 5'-phosphate (CdRP) | ||||||
Components | indole-3-glycerol phosphate synthase | ||||||
Keywords | LYASE / BETA BARREL / tryptophan biosynthesis / protein ligand complex / substrate complex | ||||||
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 / FOURIER SYNTHESIS / Resolution: 2.4 Å | ||||||
Authors | Hennig, M. / Darimont, B.D. / Kirschner, K. / Jansonius, J.N. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: The catalytic mechanism of indole-3-glycerol phosphate synthase: Crystal structures of complexes of the enzyme from Sulfolobus solfataricus with the substrate analogue, substrate, and product Authors: Hennig, M. / Darimont, B.D. / Jansonius, J.N. / Kirschner, K. #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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lbl.cif.gz | 67.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lbl.ent.gz | 49.1 KB | Display | PDB format |
PDBx/mmJSON format | 1lbl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lbl_validation.pdf.gz | 438.4 KB | Display | wwPDB validaton report |
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Full document | 1lbl_full_validation.pdf.gz | 446.1 KB | Display | |
Data in XML | 1lbl_validation.xml.gz | 8.1 KB | Display | |
Data in CIF | 1lbl_validation.cif.gz | 12.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lb/1lbl ftp://data.pdbj.org/pub/pdb/validation_reports/lb/1lbl | HTTPS FTP |
-Related structure data
Related structure data | 1a53C 1lbfC 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: 28494.906 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sulfolobus solfataricus (archaea) / Production host: Escherichia coli (E. coli) References: UniProt: Q06121, indole-3-glycerol-phosphate synthase |
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#2: Chemical | ChemComp-137 / |
#3: 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: 3.91 Å3/Da / Density % sol: 68.5 % |
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Crystal grow | Temperature: 279 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 1.2M ammonium sulphate, 50 mM potassium phosphate buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 279K |
-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-20 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 18, 1995 |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. all: 60396 / Num. obs: 17120 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.106 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: 1IGS Resolution: 2.4→15 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.4→15 Å
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Refine LS restraints |
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