+Open data
-Basic information
Entry | Database: PDB / ID: 1o5m | ||||||
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Title | Structure of FPT bound to the inhibitor SCH66336 | ||||||
Components | (Protein farnesyltransferase ...) x 2 | ||||||
Keywords | transferase/transferase inhibitor / Protein Inhibitor Complex / transferase-transferase inhibitor COMPLEX | ||||||
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 / lipid metabolic process / response to organic cyclic compound / 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 / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Strickland, C.L. / Weber, P.C. / Ganguly, A.K. | ||||||
Citation | Journal: J.Med.Chem. / Year: 1999 Title: Tricyclic Farnesyl Protein Transferase Inhibitors: Crystallographic and Calorimetric Studies of Structure-Activity Relationships Authors: Strickland, C.L. / Weber, P.C. / Windsor, W.T. / Wu, Z. / Le, H.V. / Albanese, M.M. / Alvarez, C.S. / Cesarz, D. / del Rosario, J. / Deskus, J. / Mallams, A.K. / Njoroge, F.G. / Piwinski, J. ...Authors: Strickland, C.L. / Weber, P.C. / Windsor, W.T. / Wu, Z. / Le, H.V. / Albanese, M.M. / Alvarez, C.S. / Cesarz, D. / del Rosario, J. / Deskus, J. / Mallams, A.K. / Njoroge, F.G. / Piwinski, J.J. / Remiszewski, S. / Rossman, R.R. / Taveras, A.G. / Vibulbhan, B. / Doll, R.J. / Girijavallabhan, V.M. / Ganguly, A.K. | ||||||
History |
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Remark 999 | sequence Author indicates that the sequence in the database is incorrect |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1o5m.cif.gz | 179.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1o5m.ent.gz | 138.6 KB | Display | PDB format |
PDBx/mmJSON format | 1o5m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1o5m_validation.pdf.gz | 501.3 KB | Display | wwPDB validaton report |
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Full document | 1o5m_full_validation.pdf.gz | 510.8 KB | Display | |
Data in XML | 1o5m_validation.xml.gz | 15.6 KB | Display | |
Data in CIF | 1o5m_validation.cif.gz | 28.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o5/1o5m ftp://data.pdbj.org/pub/pdb/validation_reports/o5/1o5m | HTTPS FTP |
-Related structure data
Related structure data | |
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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
-Protein farnesyltransferase ... , 2 types, 2 molecules AB
#1: Protein | Mass: 44086.090 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: FNTA / 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: 48722.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: FNTB / Production host: Escherichia coli (E. coli) References: UniProt: Q02293, Transferases; Transferring alkyl or aryl groups, other than methyl groups |
-Non-polymers , 4 types, 767 molecules
#3: Chemical | ChemComp-ZN / |
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#4: Chemical | ChemComp-FPP / |
#5: Chemical | ChemComp-336 / |
#6: 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: 3.15 Å3/Da / Density % sol: 61 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.7 Details: PEG 4000, Sodium Acetate, KCl, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 5 / Method: vapor diffusion, hanging drop / Details: Wu, Z., (1999) Protein Eng., 12, 341. | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Apr 2, 1998 / Details: MSC/Yale mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. all: 49482 / Num. obs: 49482 / % possible obs: 95.9 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.5 % / Rmerge(I) obs: 0.055 / Net I/σ(I): 23.3 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 3 % / Rmerge(I) obs: 0.212 / Num. unique all: 3673 / % possible all: 71.9 |
Reflection | *PLUS Lowest resolution: 50 Å |
Reflection shell | *PLUS % possible obs: 71.9 % / Rmerge(I) obs: 0.211 / Mean I/σ(I) obs: 4.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→8 Å / σ(F): 0.5 / Details: R-free was not used
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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