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Open data
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Basic information
Entry | Database: PDB / ID: 1hr6 | ||||||
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Title | Yeast Mitochondrial Processing Peptidase | ||||||
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![]() | HYDROLASE / HxxEH zinc-binding motif | ||||||
Function / homology | ![]() mitochondrial processing peptidase complex / mitochondrial processing peptidase / protein processing involved in protein targeting to mitochondrion / Respiratory electron transport / Mitochondrial protein degradation / endopeptidase activator activity / metalloendopeptidase activity / mitochondrial matrix / mitochondrion / proteolysis / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Taylor, A.B. / Smith, B.S. / Kitada, S. / Kojima, K. / Miyaura, H. / Otwinowski, Z. / Ito, A. / Deisenhofer, J. | ||||||
![]() | ![]() Title: Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Authors: Taylor, A.B. / Smith, B.S. / Kitada, S. / Kojima, K. / Miyaura, H. / Otwinowski, Z. / Ito, A. / Deisenhofer, 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 | ![]() | 689.3 KB | Display | ![]() |
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PDB format | ![]() | 558.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 52532.387 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PTRC99A / Species (production host): Escherichia coli / Production host: ![]() ![]() References: UniProt: P11914, mitochondrial processing peptidase #2: Protein | Mass: 48895.023 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PTRC99A / Species (production host): Escherichia coli / Production host: ![]() ![]() References: UniProt: P10507, mitochondrial processing peptidase #3: Chemical | #4: Chemical | ChemComp-ZN / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 59 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 21 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 105 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 21, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9798 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. all: 167094 / Num. obs: 167094 / % possible obs: 99.4 % / Redundancy: 6.4 % / Biso Wilson estimate: 49.2 Å2 / Rmerge(I) obs: 0.081 / Net I/σ(I): 23.6 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.541 / Mean I/σ(I) obs: 2.2 / % possible all: 97.5 |
Reflection | *PLUS Num. measured all: 1062534 |
Reflection shell | *PLUS % possible obs: 97.5 % |
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Processing
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Refinement | Resolution: 2.5→29.96 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 3556091.03 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Maximum Likelihood Function
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 33.9769 Å2 / ksol: 0.331134 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 59.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→29.96 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.5→2.59 Å / Rfactor Rfree error: 0.028 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 1.2 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 59.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.385 / % reflection Rfree: 1.2 % / Rfactor Rwork: 0.366 |