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Open data
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Basic information
Entry | Database: PDB / ID: 1ky2 | ||||||
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Title | GPPNHP-BOUND YPT7P AT 1.6 A RESOLUTION | ||||||
![]() | GTP-BINDING PROTEIN YPT7P | ||||||
![]() | ENDOCYTOSIS/EXOCYTOSIS / G PROTEIN / VESICULAR TRAFFIC / GTP HYDROLYSIS / YPT/RAB PROTEIN / ENDOCYTOSIS / HYDROLASE / ENDOCYTOSIS-EXOCYTOSIS COMPLEX | ||||||
Function / homology | ![]() RHOD GTPase cycle / TBC/RABGAPs / RHOQ GTPase cycle / RAB geranylgeranylation / vacuole-mitochondrion membrane contact site / regulation of vacuole fusion, non-autophagic / RAB GEFs exchange GTP for GDP on RABs / vacuole inheritance / protein localization to vacuole / cytoplasm to vacuole targeting by the Cvt pathway ...RHOD GTPase cycle / TBC/RABGAPs / RHOQ GTPase cycle / RAB geranylgeranylation / vacuole-mitochondrion membrane contact site / regulation of vacuole fusion, non-autophagic / RAB GEFs exchange GTP for GDP on RABs / vacuole inheritance / protein localization to vacuole / cytoplasm to vacuole targeting by the Cvt pathway / piecemeal microautophagy of the nucleus / fungal-type vacuole / retrograde transport, endosome to Golgi / vacuole / fungal-type vacuole membrane / regulation of protein-containing complex assembly / vesicle-mediated transport / Neutrophil degranulation / macroautophagy / endocytosis / late endosome / mitochondrial outer membrane / GTPase activity / protein-containing complex binding / GTP binding / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Constantinescu, A.-T. / Rak, A. / Scheidig, A.J. | ||||||
![]() | ![]() Title: Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases. Authors: Constantinescu, A.T. / Rak, A. / Alexandrov, K. / Esters, H. / Goody, R.S. / Scheidig, A.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 | ![]() | 58 KB | Display | ![]() |
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PDB format | ![]() | 39.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1ky3C ![]() 1ek0S 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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Unit cell |
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Components
#1: Protein | Mass: 20159.760 Da / Num. of mol.: 1 / Fragment: GTPASE DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: YPT7 / Plasmid: PET11 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-GNP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 44.6 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG, TRIS, GppNHp, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||
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: Nov 10, 2000 / Details: MIRROR |
Radiation | Monochromator: MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→25 Å / Num. all: 23450 / Num. obs: 23450 / % possible obs: 96.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.15 % / Biso Wilson estimate: 20.3 Å2 / Rsym value: 0.103 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 1.6→1.7 Å / Redundancy: 2.3 % / Mean I/σ(I) obs: 2.7 / Num. unique all: 3770 / Rsym value: 0.18 / % possible all: 95.7 |
Reflection | *PLUS Num. measured all: 124357 / Rmerge(I) obs: 0.103 |
Reflection shell | *PLUS Highest resolution: 1.57 Å / Lowest resolution: 1.6 Å / Rmerge(I) obs: 0.181 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1EK0 Resolution: 1.6→25 Å / Isotropic thermal model: isotropic / Cross valid method: FREE R / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-22 | |||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.4 Å2 | |||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.6→25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.6→1.7 Å / Rfactor Rfree error: 0.017
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.6 Å / % reflection Rfree: 8 % / Rfactor all: 0.1926 / Rfactor obs: 0.183 / Rfactor Rfree: 0.239 / Rfactor Rwork: 0.183 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.294 / Rfactor Rwork: 0.271 |