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- PDB-5fjx: Yeast delta-COP-I mu-homology domain complexed with Gcs1 WxxF peptide -
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Open data
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Basic information
Entry | Database: PDB / ID: 5fjx | ||||||
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Title | Yeast delta-COP-I mu-homology domain complexed with Gcs1 WxxF peptide | ||||||
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![]() | PROTEIN TRANSPORT / COP-I / VESICLE COAT PROTEIN | ||||||
Function / homology | ![]() : / Golgi localization / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / COPI vesicle coat / Golgi to plasma membrane protein transport / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / endoplasmic reticulum to Golgi vesicle-mediated transport / GTPase activator activity / trans-Golgi network ...: / Golgi localization / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / COPI vesicle coat / Golgi to plasma membrane protein transport / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / endoplasmic reticulum to Golgi vesicle-mediated transport / GTPase activator activity / trans-Golgi network / protein transport / actin binding / cytoskeleton / endosome / Golgi membrane / perinuclear region of cytoplasm / mitochondrion / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Suckling, R.J. / Evans, P.R. / Owen, D.J. | ||||||
![]() | ![]() Title: Structural Basis for the Binding of Tryptophan-Based Motifs by Delta-Cop. Authors: Suckling, R.J. / Poon, P.P. / Travis, S.M. / Majoul, I.V. / Hughson, F.M. / Evans, P.R. / Duden, R. / Owen, D.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 171.3 KB | Display | ![]() |
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PDB format | ![]() | 137.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 458 KB | Display | ![]() |
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Full document | ![]() | 462.1 KB | Display | |
Data in XML | ![]() | 31.3 KB | Display | |
Data in CIF | ![]() | 44.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5fjwSC ![]() 5fjzC ![]() 5fk0C S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 30017.650 Da / Num. of mol.: 3 / Fragment: MU-HOMOLOGY DOMAIN, RESIDUES 3282-546 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() #2: Protein/peptide | Mass: 1070.043 Da / Num. of mol.: 2 / Fragment: RESIDUES 345-352 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.57 % / Description: NONE |
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Crystal grow | pH: 8.5 / Details: 0.1M TRIS-HCL PH8.5, 0.2M MGCL2, 30% PEG-4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Aug 11, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9173 Å / Relative weight: 1 |
Reflection | Resolution: 2.45→56 Å / Num. obs: 33682 / % possible obs: 99.9 % / Observed criterion σ(I): 99 / Redundancy: 6.5 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 12.5 |
Reflection shell | Resolution: 2.45→2.55 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.9 / Mean I/σ(I) obs: 1.9 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 5FJW Resolution: 2.45→74.32 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.877 / SU B: 11.984 / SU ML: 0.263 / Cross valid method: THROUGHOUT / ESU R: 0.52 / ESU R Free: 0.324 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 59.115 Å2
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Refinement step | Cycle: LAST / Resolution: 2.45→74.32 Å
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Refine LS restraints |
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