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Open data
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Basic information
Entry | Database: PDB / ID: 1e5t | ||||||
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Title | PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT | ||||||
![]() | PROLYL ENDOPEPTIDASE | ||||||
![]() | HYDROLASE / PROLYL OLIGOPEPTIDASE / AMNESIA / ALPHA/ BETA-HYDROLASE / BETA-PROPELLER | ||||||
Function / homology | ![]() prolyl oligopeptidase / oligopeptidase activity / serine-type endopeptidase activity / proteolysis / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fulop, V. | ||||||
![]() | ![]() Title: Catalysis of Serine Oligopeptidases is Controlled by a Gating Filter Mechanism Authors: Fulop, V. / Szeltner, Z. / Polgar, L. #1: ![]() Title: Prolyl Oligopeptidase: An Unusual Beta-Propeller Domain Regulates Proteolysis Authors: Fulop, V. / Bocskei, Z. / Polgar, L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 172.6 KB | Display | ![]() |
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PDB format | ![]() | 135.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1qfmS S: Starting model for refinement |
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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: 80839.336 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-GOL / #3: Water | ChemComp-HOH / | Compound details | CHAIN A ENGINEERED MUTATION CYS255THR, GLN397CYS, LYS684MET FUNCTION: PEPTIDASE ACTIVITY ON THE C- ...CHAIN A ENGINEERED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: SEE REFERENCE, pH 8.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging dropDetails: drop consists of equal amounts of protein and reservoir solutions | ||||||||||||||||||||||||||||||||||||||||||
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: IMAGE PLATE / Date: Jul 15, 1999 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.909 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→21 Å / Num. obs: 82125 / % possible obs: 94.6 % / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Biso Wilson estimate: 14.5 Å2 / Rsym value: 0.061 / Net I/σ(I): 16.3 |
Reflection shell | Resolution: 1.4→1.76 Å / Redundancy: 3.01 % / Mean I/σ(I) obs: 1.6 / Rsym value: 0.538 / % possible all: 85.6 |
Reflection | *PLUS Num. measured all: 281721 / Rmerge(I) obs: 0.061 |
Reflection shell | *PLUS % possible obs: 85.6 % / Rmerge(I) obs: 0.538 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1QFM Resolution: 1.7→21 Å / Cross valid method: THROUGHOUT / σ(F): 2
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Displacement parameters | Biso mean: 18.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→21 Å
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Refine LS restraints |
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