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Yorodumi- PDB-1pii: THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME PHOSPHORIB... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1pii | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE: INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA COLI REFINED AT 2.0 ANGSTROMS RESOLUTION | ||||||
Components | N-(5'PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE | ||||||
Keywords | BIFUNCTIONAL(ISOMERASE AND SYNTHASE) | ||||||
Function / homology | Function and homology information phosphoribosylanthranilate isomerase / indole-3-glycerol-phosphate synthase / indole-3-glycerol-phosphate synthase activity / phosphoribosylanthranilate isomerase activity / tryptophan biosynthetic process Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Wilmanns, M. / Priestle, J.P. / Jansonius, J.N. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992 Title: Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution. Authors: Wilmanns, M. / Priestle, J.P. / Niermann, T. / Jansonius, J.N. #1: Journal: Biochemistry / Year: 1991 Title: Structural Conservation in Parallel Beta(Slash)Alpha-Barrel Enzymes that Catalyze Three Sequential Reactions in the Pathway of Tryptophan Biosynthesis Authors: Wilmanns, M. / Hyde, C.C. / Davies, D.R. / Kirschner, K. / Jansonius, J.N. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1987 Title: Three-Dimensional Structure of the Bifunctional Enzyme N-(5'-Phosphoribosyl)Anthranilate Isomerase-Indole-3-Glycerol-Phosphate Synthase from Escherichia Coli Authors: Priestle, J.P. / Gruetter, M.G. / White, J.L. / Vincent, M.G. / Kania, M. / Wilson, E. / Jardetzky, T.S. / Kirschner, K. / Jansonius, J.N. #3: Journal: FEBS Lett. / Year: 1982 Title: Crystallization and Preliminary X-Ray Crystallographic Data of the Bifunctional Enzyme Phosphoribosyl-Anthranilate Isomerase-Indole-3-Glycerol-Phosphate Synthase from Escherichia Coli Authors: White, J.L. / Gruetter, M.G. / Wilson, E. / Thaller, C. / Ford, G.C. / Smit, J.D.G. / Jansonius, J.N. / Kirschner, K. | ||||||
History |
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Remark 700 | SHEET PRAI:IGPS CONSISTS OF TWO BETA/ALPHA-BARRELS, WHICH CAN BE SUPERIMPOSED ON EACH OTHER. IGPS ...SHEET PRAI:IGPS CONSISTS OF TWO BETA/ALPHA-BARRELS, WHICH CAN BE SUPERIMPOSED ON EACH OTHER. IGPS HAS AN N-TERMINAL EXTENSION OUTSIDE OF THE BETA/ALPHA-BARREL, COMPRISING RESIDUES 1-48. THE SHEET PRESENTED AS *I* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET PRESENTED AS *P* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pii.cif.gz | 117.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pii.ent.gz | 88.9 KB | Display | PDB format |
PDBx/mmJSON format | 1pii.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pi/1pii ftp://data.pdbj.org/pub/pdb/validation_reports/pi/1pii | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES 380 - 388 HAVE VERY HIGH TEMPERATURE FACTORS. |
-Components
#1: Protein | Mass: 49412.910 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) References: UniProt: P00909, indole-3-glycerol-phosphate synthase | ||||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Compound details | THE SECONDARY STRUCTURAL ELEMENTS (ALPHA-HELICES, BETA-STRANDS, TURNS) WERE DETERMINED WITH THE ...THE SECONDARY STRUCTURAL | Sequence details | RESIDUE 329 IS IDENTIFIED AS VAL IN PIR ENTRY GWEC. RECENT RESEQUENCING CONFIRMED THAT RESIDUE 329 ...RESIDUE 329 IS IDENTIFIED | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.77 Å3/Da / Density % sol: 67.38 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusionDetails: taken from White, J.L. et al (1982). FEBS Lett., 148, 87-90. | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. obs: 45216 / % possible obs: 92.3 % / Observed criterion σ(I): 3 / Num. measured all: 130573 / Rmerge(I) obs: 0.133 |
-Processing
Software |
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Refinement | Resolution: 2→15 Å Details: THE REFINED CRYSTAL STRUCTURE OF PRAI:IGPS INCLUDES TWO PHOSPHATE IONS, ONE BOUND TO EACH ACTIVE SITE OF THIS BIFUNCTIONAL ENZYME.
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Refinement step | Cycle: LAST / Resolution: 2→15 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 15 Å / Num. reflection obs: 44611 / Rfactor obs: 0.173 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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