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- PDB-1uoq: PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1uoq | ||||||
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Title | PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, S554A MUTANT WITH BOUND PEPTIDE LIGAND GLU-PHE-SER-PRO | ||||||
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![]() | HYDROLASE / PROLYL OLIGOPEPTIDASE / AMNESIA / ALPHA/ BETA-HYDROLASE / BETA-PROPELLER / SERINE PROTEASE | ||||||
Function / homology | ![]() prolyl oligopeptidase / oligopeptidase activity / serine-type endopeptidase activity / proteolysis / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() SYNTHETIC CONSTRUCT (others) | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rea, D. / Fulop, V. | ||||||
![]() | ![]() Title: Electrostatic Environment at the Active Site of Prolyl Oligopeptidase is Highly Influential During Substrate Binding Authors: Szeltner, Z. / Rea, D. / Renner, V. / Juliano, L. / Fulop, V. / Polgar, L. #1: ![]() Title: Electrostatic Effects and Binding Determinants in the Catalysis of Prolyl Oligopeptidase: Site Specific Mutagenesis at the Oxyanion Binding Site Authors: Szeltner, Z. / Rea, D. / Renner, V. / Fulop, V. / Polgar, L. #2: ![]() Title: Substrate-Dependent Competency of the Catalytic Triad of Prolyl Oligopeptidase Authors: Szeltner, Z. / Rea, D. / Juhasz, T. / Renner, V. / Mucsi, Z. / Orosz, G. / Fulop, V. / Polgar, L. #3: ![]() Title: Structures of Prolyl Oligopeptidase Substrate/ Inhibitor Complexes. Use of Inhibitor Binding for Titration of the Catalytic Histidine Residue Authors: Fulop, V. / Szeltner, Z. / Renner, V. / Polgar, L. #4: ![]() Title: Catalysis of Serine Oligopeptidases is Controlled by a Gating Filter Mechanism Authors: Fulop, V. / Szeltner, Z. / Polgar, L. #5: ![]() Title: Prolyl Oligopeptidase: An Unusual Beta-Propeller Domain Regulates Proteolysis Authors: Fulop, V. / Bocskei, Z. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 165.1 KB | Display | ![]() |
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PDB format | ![]() | 129.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446.7 KB | Display | ![]() |
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Full document | ![]() | 454.5 KB | Display | |
Data in XML | ![]() | 32.2 KB | Display | |
Data in CIF | ![]() | 48.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1uooC ![]() 1uopC ![]() 1h2zS S: Starting model for refinement C: citing same article ( |
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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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Details | THE DIMERIC ASSEMBLY DESCRIBED HERE IS DUE TO A COMPLEXOF THE PROTEIN CHAIN A WITH A PEPTIDE (CHAIN B). CHAIN AIS ESSENTIALLY A MONOMER IN THE PHYSIOLOGICAL STATE. |
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Components
#1: Protein | Mass: 80848.344 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: ENGINEERED MUTATION SER 554 ALA / Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Protein/peptide | Mass: 478.495 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others) | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Compound details | ENGINEERED MUTATION IN CHAIN A, SER 554 ALA THE MUTATED REGION CORREPONDS TO THE ACT_SITE CHARGE ...ENGINEERED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: SEE REFERENCE 5, pH 8.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: Fulop, V., (1998) Cell(Cambridge,Mass.), 94, 161. | ||||||||||||||||||||||||||||||||||||||||||
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: ADSC CCD / Detector: CCD / Date: May 9, 2003 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→36 Å / Num. obs: 43221 / % possible obs: 95.1 % / Observed criterion σ(I): -3 / Redundancy: 3.5 % / Biso Wilson estimate: 32 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.129 / Mean I/σ(I) obs: 3.7 / % possible all: 76.8 |
Reflection | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 36 Å / Num. measured all: 153386 / Rmerge(I) obs: 0.089 |
Reflection shell | *PLUS Lowest resolution: 2.15 Å / % possible obs: 76.8 % / Rmerge(I) obs: 0.129 / Mean I/σ(I) obs: 3.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1H2Z Resolution: 2.1→36 Å / SU B: 3.663 / SU ML: 0.1 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.197 / ESU R Free: 0.173
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Displacement parameters | Biso mean: 26.4 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→36 Å
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Refinement | *PLUS % reflection Rfree: 4 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.234 / Num. reflection Rfree: 101 / Rfactor Rwork: 0.145 / Num. reflection obs: 2376 |