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- PDB-1d8d: CO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED... -

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Basic information

Entry
Database: PDB / ID: 1d8d
TitleCO-CRYSTAL STRUCTURE OF RAT PROTEIN FARNESYLTRANSFERASE COMPLEXED WITH A K-RAS4B PEPTIDE SUBSTRATE AND FPP ANALOG AT 2.0A RESOLUTION
Components
  • (farnesyltransferase ...) x 2
  • K-RAS4B PEPTIDE SUBSTRATE
KeywordsTRANSFERASE / FTASE / PFT / PFTASE / FARNESYLTRANSFERASE / FARNESYL TRANSFERASE / CAAX / RAS / CANCER
Function / homology
Function and homology information


Inactivation, recovery and regulation of the phototransduction cascade / Apoptotic cleavage of cellular proteins / RAS processing / positive regulation of tubulin deacetylation / protein geranylgeranyltransferase type I / CAAX-protein geranylgeranyltransferase activity / protein geranylgeranyltransferase activity / CAAX-protein geranylgeranyltransferase complex / protein farnesyltransferase complex / protein farnesyltransferase ...Inactivation, recovery and regulation of the phototransduction cascade / Apoptotic cleavage of cellular proteins / RAS processing / positive regulation of tubulin deacetylation / protein geranylgeranyltransferase type I / CAAX-protein geranylgeranyltransferase activity / protein geranylgeranyltransferase activity / CAAX-protein geranylgeranyltransferase complex / protein farnesyltransferase complex / protein farnesyltransferase / protein farnesyltransferase activity / neurotransmitter receptor metabolic process / regulation of fibroblast proliferation / acetylcholine receptor regulator activity / protein farnesylation / Rab geranylgeranyltransferase activity / response to inorganic substance / positive regulation of deacetylase activity / protein geranylgeranylation / protein prenylation / farnesyltranstransferase activity / negative regulation of nitric-oxide synthase biosynthetic process / endocrine signaling / forebrain astrocyte development / GMP binding / microtubule associated complex / LRR domain binding / regulation of synaptic transmission, GABAergic / epithelial tube branching involved in lung morphogenesis / response to mineralocorticoid / positive regulation of Rac protein signal transduction / alpha-tubulin binding / RAS GTPase cycle mutants / Activation of RAS in B cells / positive regulation of nitric-oxide synthase biosynthetic process / RUNX3 regulates p14-ARF / RAS signaling downstream of NF1 loss-of-function variants / response to isolation stress / SOS-mediated signalling / Activated NTRK3 signals through RAS / Activated NTRK2 signals through RAS / SHC1 events in ERBB4 signaling / homeostasis of number of cells within a tissue / Signalling to RAS / SHC-related events triggered by IGF1R / Activated NTRK2 signals through FRS2 and FRS3 / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / Signaling by FGFR3 fusions in cancer / Estrogen-stimulated signaling through PRKCZ / Signaling by PDGFRA extracellular domain mutants / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by FGFR4 in disease / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / negative regulation of cell differentiation / positive regulation of cell cycle / Signaling by FLT3 ITD and TKD mutants / Erythropoietin activates RAS / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR3 signaling / Tie2 Signaling / Signaling by CSF3 (G-CSF) / Signaling by FGFR3 point mutants in cancer / G protein activity / FRS-mediated FGFR2 signaling / small monomeric GTPase / FRS-mediated FGFR4 signaling / Signaling by FGFR2 in disease / Ras activation upon Ca2+ influx through NMDA receptor / FRS-mediated FGFR1 signaling / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / Signaling by FLT3 fusion proteins / FLT3 Signaling / p38MAPK events / EGFR Transactivation by Gastrin / Signaling by FGFR1 in disease / GRB2 events in ERBB2 signaling / CD209 (DC-SIGN) signaling / Downstream signal transduction / striated muscle cell differentiation / SHC1 events in ERBB2 signaling / Insulin receptor signalling cascade / NCAM signaling for neurite out-growth / Constitutive Signaling by Overexpressed ERBB2 / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / visual learning / VEGFR2 mediated cell proliferation / Ca2+ pathway / response to cytokine / response to glucocorticoid / regulation of long-term neuronal synaptic plasticity / RAF activation / Signaling by high-kinase activity BRAF mutants / FCERI mediated MAPK activation / positive regulation of fibroblast proliferation / Signaling by ERBB2 TMD/JMD mutants / MAP2K and MAPK activation
Similarity search - Function
Protein farnesyltransferase subunit beta / Protein prenylyltransferase / Protein prenyltransferase alpha subunit repeat / Protein prenyltransferases alpha subunit repeat profile. / Protein prenyltransferase, alpha subunit / PFTB repeat / Prenyltransferase and squalene oxidase repeat / Glycosyltransferase - #20 / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Small GTPase, Ras-type ...Protein farnesyltransferase subunit beta / Protein prenylyltransferase / Protein prenyltransferase alpha subunit repeat / Protein prenyltransferases alpha subunit repeat profile. / Protein prenyltransferase, alpha subunit / PFTB repeat / Prenyltransferase and squalene oxidase repeat / Glycosyltransferase - #20 / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Small GTPase, Ras-type / small GTPase Ras family profile. / Glycosyltransferase / Alpha/alpha barrel / Rho (Ras homology) subfamily of Ras-like small GTPases / Small GTPase / Ras family / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Small GTP-binding protein domain / Alpha Horseshoe / P-loop containing nucleoside triphosphate hydrolase / Mainly Alpha
Similarity search - Domain/homology
Protein farnesyltransferase subunit beta / ACETATE ION / GTPase KRas / Chem-FII / Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / Resolution: 2 Å
AuthorsLong, S.B. / Casey, P.J. / Beese, L.S.
Citation
Journal: Structure Fold.Des. / Year: 2000
Title: The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures.
Authors: Long, S.B. / Casey, P.J. / Beese, L.S.
#1: Journal: Science / Year: 1997
Title: Crystal Structure of Protein Farnesyltransferase at 2.25A Resolution
Authors: Park, H.-W. / Boduluri, S.R. / Moomaw, J.F. / Casey, P.J. / Beese, L.S.
#2: Journal: Biochemistry / Year: 1998
Title: Co-crystal Structure of Mammalian Protein Farnesyltransferase with a Farnesyl Diphosphate Substrate
Authors: Long, S.B. / Casey, P.J. / Beese, L.S.
History
DepositionOct 22, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 9, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: farnesyltransferase (alpha subunit)
B: farnesyltransferase (beta subunit)
P: K-RAS4B PEPTIDE SUBSTRATE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,7809
Polymers94,1193
Non-polymers6616
Water8,053447
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10670 Å2
ΔGint-69 kcal/mol
Surface area29150 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)170.919, 170.919, 69.284
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number169
Space group name H-MP61

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Components

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Farnesyltransferase ... , 2 types, 2 molecules AB

#1: Protein farnesyltransferase (alpha subunit) / FTASE


Mass: 44098.145 Da / Num. of mol.: 1 / Fragment: alpha subunit
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: BRAIN / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q04631, squalene synthase
#2: Protein farnesyltransferase (beta subunit) / FTASE


Mass: 48722.281 Da / Num. of mol.: 1 / Fragment: beta subunit
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: BRAIN / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q02293, squalene synthase

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Protein/peptide , 1 types, 1 molecules P

#3: Protein/peptide K-RAS4B PEPTIDE SUBSTRATE


Mass: 1298.723 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: This synthetic peptide is derived from human K-Ras4B, residues 178-188.
References: UniProt: P01116

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Non-polymers , 4 types, 453 molecules

#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#5: Chemical
ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H3O2
Details: non-reactive FPP analog (FPT Inhibitor II, Calbiochem) Manne, V. et al. & Biller, S.A. (1995) Drug Dev. Res. 34,pg 121-137
#6: Chemical ChemComp-FII / [(3,7,11-TRIMETHYL-DODECA-2,6,10-TRIENYLOXYCARBAMOYL)-METHYL]-PHOSPHONIC ACID / FPP ANALOG


Mass: 359.398 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H30NO5P
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 447 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.1 Å3/Da / Density % sol: 60.35 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop / pH: 5.7
Details: Peg 8000, ammonium acetate, DTT, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Crystal grow
*PLUS
Temperature: 17 ℃
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
112-16 %(w/v)PEG80001reservoir
2600 mMammonium acetate1reservoir
320 mMdithiothreitol1reservoir

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Data collection

DiffractionMean temperature: 96 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Oct 23, 1998
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2→35 Å / Num. all: 77998 / Num. obs: 76088 / % possible obs: 97.5 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 27.1 Å2 / Rmerge(I) obs: 0.045 / Net I/σ(I): 13.9
Reflection shellResolution: 2→2.02 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.197 / Num. unique all: 2154 / % possible all: 83.9
Reflection
*PLUS
Num. measured all: 320401
Reflection shell
*PLUS
% possible obs: 83.9 %

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Processing

Software
NameVersionClassification
X-PLOR3.851model building
X-PLOR3.851refinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLOR3.851phasing
RefinementResolution: 2→35 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): -3 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2 3698 5.1 %RANDOM
Rwork0.164 ---
all0.171 76088 --
obs0.166 73152 93.6 %-
Displacement parametersBiso mean: 34.2 Å2
Baniso -1Baniso -2Baniso -3
1-0.247 Å21.184 Å20 Å2
2--0.247 Å20 Å2
3---5.753 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.24 Å0.2 Å
Luzzati d res low-5 Å
Luzzati sigma a0.22 Å0.22 Å
Refinement stepCycle: LAST / Resolution: 2→35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6037 0 41 447 6525
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_angle_deg1.4
X-RAY DIFFRACTIONx_dihedral_angle_d21.3
X-RAY DIFFRACTIONx_improper_angle_d1.35
LS refinement shellResolution: 2→2.09 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 8
RfactorNum. reflection% reflection
Rfree0.265 398 5.2 %
Rwork0.24 7321 -
obs--79.5 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2PARAM19.SOLTOP
X-RAY DIFFRACTION3TOPH19.SOL
X-RAY DIFFRACTION4ACE.SOL
X-RAY DIFFRACTION5
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg21.3
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.35

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