+Open data
-Basic information
Entry | Database: PDB / ID: 1z0d | ||||||
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Title | GDP-Bound Rab5c GTPase | ||||||
Components | Ras-related protein Rab-5C | ||||||
Keywords | PROTEIN TRANSPORT / Rab GTPase / Rab5c / vesicular trafficking | ||||||
Function / homology | Function and homology information RAB geranylgeranylation / RAB GEFs exchange GTP for GDP on RABs / Golgi Associated Vesicle Biogenesis / endosome organization / Clathrin-mediated endocytosis / regulation of endocytosis / endocytic vesicle / endomembrane system / Neutrophil degranulation / small monomeric GTPase ...RAB geranylgeranylation / RAB GEFs exchange GTP for GDP on RABs / Golgi Associated Vesicle Biogenesis / endosome organization / Clathrin-mediated endocytosis / regulation of endocytosis / endocytic vesicle / endomembrane system / Neutrophil degranulation / small monomeric GTPase / intracellular protein transport / G protein activity / synaptic vesicle membrane / endocytosis / GDP binding / melanosome / early endosome membrane / GTPase activity / GTP binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Eathiraj, S. / Pan, X. / Ritacco, C. / Lambright, D.G. | ||||||
Citation | Journal: Nature / Year: 2005 Title: Structural basis of family-wide Rab GTPase recognition by rabenosyn-5. Authors: Eathiraj, S. / Pan, X. / Ritacco, C. / Lambright, D.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z0d.cif.gz | 89 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1z0d.ent.gz | 65.4 KB | Display | PDB format |
PDBx/mmJSON format | 1z0d.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1z0d_validation.pdf.gz | 1014.1 KB | Display | wwPDB validaton report |
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Full document | 1z0d_full_validation.pdf.gz | 1015.8 KB | Display | |
Data in XML | 1z0d_validation.xml.gz | 19.4 KB | Display | |
Data in CIF | 1z0d_validation.cif.gz | 28.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z0/1z0d ftp://data.pdbj.org/pub/pdb/validation_reports/z0/1z0d | HTTPS FTP |
-Related structure data
Related structure data | 1yu9C 1yvdC 1yzkC 1yzlC 1yzmC 1yznC 1yzqC 1yztC 1yzuC 1z06C 1z07C 1z08C 1z0aC 1z0fC 1z0iC 1z0jC 1z0kC 1z22C 1z2aC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 18500.102 Da / Num. of mol.: 2 / Fragment: GTPase domain / Mutation: Q80L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Rab5c / Plasmid: pGEX4T1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) Codon Plus-RIL Cells / References: UniProt: P35278 #2: Chemical | ChemComp-PO4 / | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.46 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 10% PEG 4000, 200mM Lithium Sulfate, 50mM Na acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418 |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Aug 4, 2004 / Details: Osmic mirror |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 19641 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5 % / Biso Wilson estimate: 37.5 Å2 / Rsym value: 0.088 / Net I/σ(I): 17 |
Reflection shell | Resolution: 2.2→2.26 Å / Redundancy: 5 % / Mean I/σ(I) obs: 4 / Num. unique all: 1609 / Rsym value: 0.407 / % possible all: 97.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Polyalanine Rab3A GTPase Resolution: 2.2→8 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.914 / SU B: 5.505 / SU ML: 0.144 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.29 / ESU R Free: 0.225 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 28.211 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.253 Å / Total num. of bins used: 20
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