+Open data
-Basic information
Entry | Database: PDB / ID: 1o1r | ||||||
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Title | Structure of FPT bound to GGPP | ||||||
Components |
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Keywords | TRANSFERASE / Prenyltransferase | ||||||
Function / homology | Function and homology information Apoptotic cleavage of cellular proteins / Inactivation, recovery and regulation of the phototransduction cascade / RAS processing / protein geranylgeranyltransferase activity / protein geranylgeranyltransferase type I / CAAX-protein geranylgeranyltransferase activity / CAAX-protein geranylgeranyltransferase complex / protein farnesylation / positive regulation of tubulin deacetylation / protein farnesyltransferase ...Apoptotic cleavage of cellular proteins / Inactivation, recovery and regulation of the phototransduction cascade / RAS processing / protein geranylgeranyltransferase activity / protein geranylgeranyltransferase type I / CAAX-protein geranylgeranyltransferase activity / CAAX-protein geranylgeranyltransferase complex / protein farnesylation / positive regulation of tubulin deacetylation / protein farnesyltransferase / protein farnesyltransferase activity / protein farnesyltransferase complex / regulation of fibroblast proliferation / Rab geranylgeranyltransferase activity / protein geranylgeranylation / positive regulation of skeletal muscle acetylcholine-gated channel clustering / negative regulation of nitric-oxide synthase biosynthetic process / farnesyltranstransferase activity / microtubule associated complex / enzyme-linked receptor protein signaling pathway / positive regulation of nitric-oxide synthase biosynthetic process / positive regulation of Rac protein signal transduction / alpha-tubulin binding / : / positive regulation of cell cycle / response to cytokine / wound healing / response to organic cyclic compound / lipid metabolic process / receptor tyrosine kinase binding / positive regulation of fibroblast proliferation / fibroblast proliferation / microtubule binding / cell population proliferation / molecular adaptor activity / negative regulation of cell population proliferation / positive regulation of cell population proliferation / negative regulation of apoptotic process / zinc ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Turek-Etienne, T.C. / Strickland, C.L. / Distefano, M.D. | ||||||
Citation | Journal: Biochemistry / Year: 2003 Title: Biochemical and Structural Studies with Prenyl Diphosphate Analogues Provide Insights into Isoprenoid Recognition by Protein Farnesyl Transferase Authors: Turek-Etienne, T.C. / Strickland, C.L. / Distefano, M.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1o1r.cif.gz | 177.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1o1r.ent.gz | 137.1 KB | Display | PDB format |
PDBx/mmJSON format | 1o1r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1o1r_validation.pdf.gz | 427.4 KB | Display | wwPDB validaton report |
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Full document | 1o1r_full_validation.pdf.gz | 438.4 KB | Display | |
Data in XML | 1o1r_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 1o1r_validation.cif.gz | 28.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o1/1o1r ftp://data.pdbj.org/pub/pdb/validation_reports/o1/1o1r | HTTPS FTP |
-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: 44368.359 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pET15b / Production host: Escherichia coli (E. coli) References: UniProt: Q04631, Transferases; Transferring alkyl or aryl groups, other than methyl groups |
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#2: Protein | Mass: 47749.340 Da / Num. of mol.: 1 / Fragment: residue 1-427 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pET15b / Production host: Escherichia coli (E. coli) References: UniProt: Q02293, Transferases; Transferring alkyl or aryl groups, other than methyl groups |
#3: Chemical | ChemComp-ZN / |
#4: Chemical | ChemComp-GRG / |
#5: 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: 3.19 Å3/Da / Density % sol: 61.41 % |
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Crystal grow | Temperature: 298 K / Method: hanging drop / pH: 5.7 Details: PEG 4000, Sodium Acetate, KCl, pH 5.7, hanging drop, temperature 298.0K |
Crystal grow | *PLUS Method: unknown |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Nov 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. all: 51180 / Num. obs: 51180 / % possible obs: 99.3 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 24.1 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.367 / Num. unique all: 5114 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Resolution: 2.3→8 Å
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refinement | *PLUS | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |