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- PDB-1mzc: Co-Crystal Structure Of Human Farnesyltransferase With Farnesyldi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mzc | |||||||||
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Title | Co-Crystal Structure Of Human Farnesyltransferase With Farnesyldiphosphate and Inhibitor Compound 33a | |||||||||
![]() | (Protein Farnesyltransferase ...) x 2 | |||||||||
![]() | TRANSFERASE / ALPHA-ALPHA BARREL / INHIBITOR / FTASE / PFTASE / FPP / CAAX / RAS | |||||||||
Function / homology | ![]() positive regulation of deacetylase activity / skeletal muscle acetylcholine-gated channel clustering / 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 ...positive regulation of deacetylase activity / skeletal muscle acetylcholine-gated channel clustering / 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 / Rab geranylgeranyltransferase activity / protein geranylgeranylation / positive regulation of skeletal muscle acetylcholine-gated channel clustering / microtubule associated complex / Apoptotic cleavage of cellular proteins / positive regulation of Rac protein signal transduction / alpha-tubulin binding / transforming growth factor beta receptor signaling pathway / lipid metabolic process / receptor tyrosine kinase binding / RAS processing / Inactivation, recovery and regulation of the phototransduction cascade / microtubule binding / Potential therapeutics for SARS / molecular adaptor activity / zinc ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | deSolms, S.J. / Ciccarone, T.M. / MacTough, S.C. / Shaw, A.W. / Buser, C.A. / Ellis-Hutchings, M. / Fernandes, C. / Hamilton, K.A. / Huber, H.E. / Kohl, N.E. ...deSolms, S.J. / Ciccarone, T.M. / MacTough, S.C. / Shaw, A.W. / Buser, C.A. / Ellis-Hutchings, M. / Fernandes, C. / Hamilton, K.A. / Huber, H.E. / Kohl, N.E. / Lobell, R.B. / Robinson, R.G. / Tsou, N.N. / Walsh, E.S. / Graham, S.L. / Beese, L.S. / Taylor, J.S. | |||||||||
![]() | ![]() Title: Dual Protein Farnesyltransferase-Geranylgeranyltransferase-I Inhibitors as Potential Cancer Chemotherapeutic Agents. Authors: DeSolms, S.J. / Ciccarone, T.M. / MacTough, S.C. / Shaw, A.W. / Buser, C.A. / Ellis-Hutchings, M. / Fernandes, C. / Hamilton, K.A. / Huber, H.E. / Kohl, N.E. / Lobell, R.B. / Robinson, R.G. ...Authors: DeSolms, S.J. / Ciccarone, T.M. / MacTough, S.C. / Shaw, A.W. / Buser, C.A. / Ellis-Hutchings, M. / Fernandes, C. / Hamilton, K.A. / Huber, H.E. / Kohl, N.E. / Lobell, R.B. / Robinson, R.G. / Tsou, N.N. / Walsh, E.S. / Graham, S.L. / Beese, L.S. / Taylor, J.S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 180.7 KB | Display | ![]() |
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PDB format | ![]() | 137.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 35.6 KB | Display | |
Data in CIF | ![]() | 53.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1jcqS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | The asymmetric unit contains one complete biological unit (heterodimer) |
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Components
-Protein Farnesyltransferase ... , 2 types, 2 molecules AB
#1: Protein | Mass: 44864.840 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P49354, Transferases; Transferring alkyl or aryl groups, other than methyl groups |
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#2: Protein | Mass: 48822.406 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P49356, Transferases; Transferring alkyl or aryl groups, other than methyl groups |
-Sugars , 1 types, 1 molecules
#3: Polysaccharide | beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose |
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-Non-polymers , 4 types, 706 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/FPP.gif)
![](data/chem/img/BNE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FPP.gif)
![](data/chem/img/BNE.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-ZN / |
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#5: Chemical | ChemComp-FPP / |
#6: Chemical | ChemComp-BNE / |
#7: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.16 Å3/Da / Density % sol: 61.13 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: PEG8K NH4OAc, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 17 ℃ / Method: vapor diffusion, hanging drop / PH range low: 5.5 / PH range high: 5.3 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 17, 2000 / Details: Mirrors |
Radiation | Monochromator: YALE MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→36.7 Å / Num. all: 75205 / Num. obs: 75205 / % possible obs: 94.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Biso Wilson estimate: 14.1 Å2 / Rsym value: 0.078 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 2→2.03 Å / Mean I/σ(I) obs: 2.1 / Num. unique all: 3242 / Rsym value: 0.341 / % possible all: 82.1 |
Reflection | *PLUS Lowest resolution: 37 Å / % possible obs: 94.7 % / Num. measured all: 278618 / Rmerge(I) obs: 0.078 |
Reflection shell | *PLUS % possible obs: 82.4 % / Rmerge(I) obs: 0.341 / Mean I/σ(I) obs: 2.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1JCQ Resolution: 2→36.7 Å / Rfactor Rfree error: 0.003 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 57.8835 Å2 / ksol: 0.399425 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→36.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.13 Å / Rfactor Rfree error: 0.011 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 37 Å / Rfactor Rfree: 0.208 / Rfactor Rwork: 0.179 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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