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- PDB-3w1s: Crystal structure of Saccharomyces cerevisiae Atg12-Atg5 conjugat... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3w1s | ||||||
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Title | Crystal structure of Saccharomyces cerevisiae Atg12-Atg5 conjugate bound to the N-terminal domain of Atg16 | ||||||
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![]() | LIGASE / Ubiquitin fold / E3-like / Atg3 binding / Isopeptide bond between Atg12 Gly186 and Atg5 Lys149 | ||||||
Function / homology | ![]() protein lipidation involved in autophagosome assembly / : / cargo receptor ligand activity / Receptor Mediated Mitophagy / Atg8-family ligase activity / Atg12-Atg5-Atg16 complex / C-terminal protein lipidation / phagophore / vacuole-isolation membrane contact site / Macroautophagy ...protein lipidation involved in autophagosome assembly / : / cargo receptor ligand activity / Receptor Mediated Mitophagy / Atg8-family ligase activity / Atg12-Atg5-Atg16 complex / C-terminal protein lipidation / phagophore / vacuole-isolation membrane contact site / Macroautophagy / mitochondria-associated endoplasmic reticulum membrane contact site / transferase complex / cytoplasm to vacuole targeting by the Cvt pathway / nucleophagy / autophagosome organization / autophagy of mitochondrion / phagophore assembly site membrane / piecemeal microautophagy of the nucleus / cellular response to nitrogen starvation / phagophore assembly site / mitophagy / autophagosome assembly / autophagosome / enzyme activator activity / macroautophagy / autophagy / protein tag activity / protein-macromolecule adaptor activity / hydrolase activity / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Noda, N.N. / Fujioka, Y. / Hanada, T. / Ohsumi, Y. / Inagaki, F. | ||||||
![]() | ![]() Title: Structure of the Atg12-Atg5 conjugate reveals a platform for stimulating Atg8-PE conjugation Authors: Noda, N.N. / Fujioka, Y. / Hanada, T. / Ohsumi, Y. / Inagaki, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86.3 KB | Display | ![]() |
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PDB format | ![]() | 64.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446.3 KB | Display | ![]() |
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Full document | ![]() | 454.1 KB | Display | |
Data in XML | ![]() | 15.5 KB | Display | |
Data in CIF | ![]() | 20.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 32620.820 Da / Num. of mol.: 1 / Fragment: UNP residues 1-284 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 5792.501 Da / Num. of mol.: 1 / Fragment: UNP residues 1-46 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: APG15, APG16, ATG16, Atg16(amino acids 1-46), CVT11, SAP18, YM8520.08C, YMR159C Plasmid: pGEX6p / Production host: ![]() ![]() |
#3: Protein | Mass: 10341.172 Da / Num. of mol.: 1 / Fragment: UNP residues 100-186 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: APG12, ATG12, Atg12(amino acids 100-186), YBR1506, YBR217W Plasmid: pACYC184 / Production host: ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 56.19 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 12% PEG10000, 0.5M potassium thiocyanate, 0.1M ADA, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 3, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→42.6 Å / Num. all: 17196 / Num. obs: 17173 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 7.3 % / Biso Wilson estimate: 53.8 Å2 / Rsym value: 0.055 / Net I/σ(I): 9.6 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 7.4 % / Num. unique all: 1691 / Rsym value: 0.303 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2DYM, 1WZ3 Resolution: 2.6→42.6 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 167335.04 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: BULK SOLVENT MODEL USED
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 48.3649 Å2 / ksol: 0.38 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 51.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→42.6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.022 / Total num. of bins used: 6
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Xplor file |
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