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- PDB-1nzn: Cytosolic domain of the human mitchondrial fission protein Fis1 a... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1nzn | ||||||
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Title | Cytosolic domain of the human mitchondrial fission protein Fis1 adopts a TPR fold | ||||||
![]() | Fission protein Fis1p | ||||||
![]() | UNKNOWN FUNCTION / TPR | ||||||
Function / homology | ![]() negative regulation of fatty acid transport / negative regulation of ATP metabolic process / Class I peroxisomal membrane protein import / positive regulation of mitochondrial calcium ion concentration / peroxisome fission / mitochondrial fragmentation involved in apoptotic process / negative regulation of endoplasmic reticulum calcium ion concentration / autophagy of mitochondrion / protein targeting to mitochondrion / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gittis, A.G. / Dohm, J.A. / Hill, R.B. | ||||||
![]() | ![]() Title: Cytosolic domain of the human mitchondrial fission protein Fis1 adopts a TPR fold Authors: Dohm, J.A. / Lee, S.J. / Hardwick, J.M. / Hill, R.B. / Gittis, A.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 34.1 KB | Display | ![]() |
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PDB format | ![]() | 26.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar 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 on special symmetry positions |
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Components
#1: Protein | Mass: 14767.588 Da / Num. of mol.: 1 / Fragment: cytosolic fragment Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / ![]() |
#3: Chemical | ChemComp-GOL / ![]() |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 38.01 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: Ammonium Sulphate, Sodium Acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: SBC-2 / Detector: CCD / Date: Dec 13, 2002 |
Radiation | Monochromator: Si 220 / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2→25 Å / Num. all: 8523 / Num. obs: 8523 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7 % / Biso Wilson estimate: 24.36 Å2 / Rmerge(I) obs: 0.048 |
Reflection shell | Resolution: 2→2.05 Å / % possible all: 99.8 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 20 Å / Num. obs: 7912 / % possible obs: 99.7 % / Redundancy: 7 % / Rmerge(I) obs: 0.044 |
Reflection shell | *PLUS Mean I/σ(I) obs: 26.8 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 20 Å / % reflection Rfree: 8 % / Rfactor Rfree![]() ![]() | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |