+Open data
-Basic information
Entry | Database: PDB / ID: 5jh9 | ||||||
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Title | Crystal structure of prApe1 | ||||||
Components | Vacuolar aminopeptidase 1 | ||||||
Keywords | HYDROLASE / Tetrahedral dodecamer | ||||||
Function / homology | Function and homology information aminopeptidase I / Cvt complex / cytoplasm to vacuole targeting by the Cvt pathway / fungal-type vacuole / metalloaminopeptidase activity / protein transport / proteolysis / zinc ion binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Noda, N.N. / Adachi, W. / Inagaki, F. | ||||||
Citation | Journal: Cell Rep / Year: 2016 Title: Structural Basis for Receptor-Mediated Selective Autophagy of Aminopeptidase I Aggregates Authors: Yamasaki, A. / Watanabe, Y. / Adachi, W. / Suzuki, K. / Matoba, K. / Kirisako, H. / Kumeta, H. / Nakatogawa, H. / Ohsumi, Y. / Inagaki, F. / Noda, N.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5jh9.cif.gz | 743 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5jh9.ent.gz | 619.2 KB | Display | PDB format |
PDBx/mmJSON format | 5jh9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jh/5jh9 ftp://data.pdbj.org/pub/pdb/validation_reports/jh/5jh9 | HTTPS FTP |
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-Related structure data
Related structure data | 5jgeC 5jgfSC 5jhcC C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 57290.516 Da / Num. of mol.: 4 / Mutation: L11S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Strain: ATCC 204508 / S288c / Gene: APE1, API, LAP4, YSC1, YKL103C, YKL455 / Production host: Escherichia coli (E. coli) / References: UniProt: P14904, aminopeptidase I #2: Chemical | ChemComp-ZN / #3: Chemical | ChemComp-CAC / #4: 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: 2.89 Å3/Da / Density % sol: 57.43 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 50% (v/v) PEG 200, 200 mM Magnesium chloride, 100 mM sodium cacodylate |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 16, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→500 Å / Num. obs: 123984 / % possible obs: 100 % / Redundancy: 5.4 % / Rmerge(I) obs: 0.045 / Net I/σ(I): 20.3 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 5 % / Rmerge(I) obs: 0.19 / Mean I/σ(I) obs: 5.4 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5JGF Resolution: 2.1→44.79 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.936 / SU B: 7.623 / SU ML: 0.108 / Cross valid method: THROUGHOUT / ESU R: 0.202 / ESU R Free: 0.164 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 36.387 Å2
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Refinement step | Cycle: 1 / Resolution: 2.1→44.79 Å
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Refine LS restraints |
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