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- PDB-1f60: CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA -
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Open data
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Basic information
Entry | Database: PDB / ID: 1f60 | ||||||
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Title | CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA | ||||||
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![]() | TRANSLATION / protein-protein complex | ||||||
Function / homology | ![]() Eukaryotic Translation Elongation / eukaryotic translation elongation factor 1 complex / negative regulation of actin filament bundle assembly / HSF1 activation / melatonin binding / regulation of translational termination / tRNA export from nucleus / sulfur compound metabolic process / Protein methylation / fungal-type vacuole membrane ...Eukaryotic Translation Elongation / eukaryotic translation elongation factor 1 complex / negative regulation of actin filament bundle assembly / HSF1 activation / melatonin binding / regulation of translational termination / tRNA export from nucleus / sulfur compound metabolic process / Protein methylation / fungal-type vacuole membrane / translational elongation / actin filament bundle assembly / translation elongation factor activity / Neutrophil degranulation / cellular response to amino acid starvation / guanyl-nucleotide exchange factor activity / negative regulation of protein phosphorylation / maintenance of translational fidelity / negative regulation of protein kinase activity / GDP binding / actin filament binding / ribosome binding / cytoskeleton / ribosome / translation / GTPase activity / GTP binding / protein kinase binding / mitochondrion / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Andersen, G.R. / Pedersen, L. / Valente, L. / Kinzy, T.G. / Nyborg, J. | ||||||
![]() | ![]() Title: Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. Authors: Andersen, G.R. / Pedersen, L. / Valente, L. / Chatterjee, I. / Kinzy, T.G. / Kjeldgaard, M. / Nyborg, J. #1: ![]() Title: The Solution Structure of the Guanine Nucleotide Exchange Domain of Human Elongation Factor 1beta Reveals a Striking Resemblance to that of EF-Ts from Escherichia coli Authors: Perez, J.M. / Siegal, G. / Kriek, J. / Hard, K. / Dijk, J. / Canters, G.W. / Moeller, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 130.8 KB | Display | ![]() |
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PDB format | ![]() | 99.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.5 KB | Display | ![]() |
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Full document | ![]() | 445.1 KB | Display | |
Data in XML | ![]() | 28.8 KB | Display | |
Data in CIF | ![]() | 44.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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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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Components
#1: Protein | Mass: 50110.621 Da / Num. of mol.: 1 / Fragment: EEF1A / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 10472.829 Da / Num. of mol.: 1 / Fragment: EEF1BA, CATALYTICAL C-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PET11D / Production host: ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.29 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: mmE 2000, Tris, Hepes, KCl, DTT, NaAzid, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 4K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K / pH: 7.2 Details: Pedersen, L.P., (2000) Acta Crystallogr., D57, 159. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: MARRESEARCH / Detector: CCD / Date: Mar 1, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 1.67→20 Å / Num. all: 65533 / Num. obs: 65533 / % possible obs: 99.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Biso Wilson estimate: 16.8 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 36.1 |
Reflection shell | Resolution: 1.67→1.73 Å / Redundancy: 3 % / Rmerge(I) obs: 0.155 / Num. unique all: 5881 / % possible all: 93.5 |
Reflection | *PLUS |
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Processing
Software |
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Refinement | Resolution: 1.67→20 Å / σ(F): 0 / σ(I): 0 Stereochemistry target values: engh & huber in arp_protin.doc Details: Refmac conjugate direction method
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Refinement step | Cycle: LAST / Resolution: 1.67→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 0 / Rfactor obs: 0.187 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_angle_d / Dev ideal: 1.6 |