+Open data
-Basic information
Entry | Database: PDB / ID: 1ubw | ||||||
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Title | STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE | ||||||
Components | FARNESYL DIPHOSPHATE SYNTHASE | ||||||
Keywords | TRANSFERASE / ISOPRENE BIOSYNTHESIS / CHOLESTEROL BIOSYNTHESIS | ||||||
Function / homology | Function and homology information geranyl diphosphate biosynthetic process / dimethylallyltranstransferase / (2E,6E)-farnesyl diphosphate synthase / farnesyl diphosphate biosynthetic process / dimethylallyltranstransferase activity / geranyltranstransferase activity / cholesterol biosynthetic process / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Tarshis, L.C. / Proteau, P. / Poulter, C.D. / Sacchettini, J.C. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1996 Title: Regulation of product chain length by isoprenyl diphosphate synthases. Authors: Tarshis, L.C. / Proteau, P.J. / Kellogg, B.A. / Sacchettini, J.C. / Poulter, C.D. #1: Journal: Biochemistry / Year: 1994 Title: Crystal Structure of Recombinant Farnesyl Diphosphate Synthase at 2.6-A Resolution Authors: Tarshis, L.C. / Yan, M. / Poulter, C.D. / Sacchettini, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ubw.cif.gz | 85.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ubw.ent.gz | 64.5 KB | Display | PDB format |
PDBx/mmJSON format | 1ubw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ub/1ubw ftp://data.pdbj.org/pub/pdb/validation_reports/ub/1ubw | HTTPS FTP |
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-Related 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: 42013.004 Da / Num. of mol.: 1 / Mutation: F112A, F113S Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH GERANYL DIPHOSPHATE AND MAGNESIUM / Source: (gene. exp.) Gallus gallus (chicken) / Organ: LIVER / Plasmid: PUC / Production host: Escherichia coli (E. coli) / References: UniProt: P08836, dimethylallyltranstransferase | ||||
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#2: Chemical | #3: Chemical | ChemComp-GPP / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.22 Å3/Da / Density % sol: 61.76 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: unknown | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Date: Jul 31, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 19489 / % possible obs: 89 % / Observed criterion σ(I): 0.2 / Redundancy: 3 % / Rmerge(I) obs: 0.068 |
-Processing
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Refinement | Highest resolution: 2.5 Å / Num. reflection obs: 17007 / σ(F): 2 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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Refine LS restraints |
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