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Yorodumi- PDB-2ptn: ON THE DISORDERED ACTIVATION DOMAIN IN TRYPSINOGEN. CHEMICAL LABE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ptn | |||||||||
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Title | ON THE DISORDERED ACTIVATION DOMAIN IN TRYPSINOGEN. CHEMICAL LABELLING AND LOW-TEMPERATURE CRYSTALLOGRAPHY | |||||||||
Components | TRYPSIN | |||||||||
Keywords | HYDROLASE (SERINE PROTEINASE) | |||||||||
Function / homology | Function and homology information trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | |||||||||
Biological species | Bos taurus (cattle) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.55 Å | |||||||||
Authors | Walter, J. / Steigemann, W. / Singh, T.P. / Bartunik, H. / Bode, W. / Huber, R. | |||||||||
Citation | Journal: Acta Crystallogr.,Sect.B / Year: 1982 Title: On the Disordered Activation Domain in Trypsinogen. Chemical Labelling and Low-Temperature Crystallography Authors: Walter, J. / Steigemann, W. / Singh, T.P. / Bartunik, H. / Bode, W. / Huber, R. #1: Journal: Acta Crystallogr.,Sect.B / Year: 1983 Title: The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors Authors: Marquart, M. / Walter, J. / Deisenhofer, J. / Bode, W. / Huber, R. #2: Journal: Miami Winter Symp. / Year: 1976 Title: Structural Studies on the Pancreatic Trypsin Inhibitor-Trypsin Complex and its Free Components. Structure and Function Relationships in Serine Protease Inhibition and Catalysis Authors: Bode, W. / Schwager, P. / Huber, R. #3: Journal: J.Mol.Biol. / Year: 1975 Title: The Refined Crystal Structure of Bovine Beta-Trypsin at 1.8 Angstroms Resolution. II. Crystallographic Refinement, Calcium Binding Site, Benzamidine Binding Site and Active Site at Ph 7.0 Authors: Bode, W. / Schwager, P. #4: Journal: J.Mol.Biol. / Year: 1975 Title: The Refined Crystal Structure of Bovine Beta-Trypsin at 1.8 Angstroms Resolution. I. Crystallization, Data Collection and Application of Patterson Search Techniques Authors: Fehlhammer, H. / Bode, W. #5: Journal: FEBS Lett. / Year: 1975 Title: The Single Calcium-Binding Site of Crystalline Bovine Beta-Trypsin Authors: Bode, W. / Schwager, P. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ptn.cif.gz | 48.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ptn.ent.gz | 38.3 KB | Display | PDB format |
PDBx/mmJSON format | 2ptn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pt/2ptn ftp://data.pdbj.org/pub/pdb/validation_reports/pt/2ptn | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: SEE REMARK 4. |
-Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P00760, trypsin |
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#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.16 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.55 Å |
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-Processing
Refinement | Resolution: 1.55→6.5 Å / Rfactor Rwork: 0.193 | ||||||||||||
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Refinement step | Cycle: LAST / Resolution: 1.55→6.5 Å
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Refinement | *PLUS Num. reflection obs: 23560 / Highest resolution: 1.55 Å / Lowest resolution: 6.5 Å / Rfactor obs: 0.193 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS Biso mean: 14.5 Å2 | ||||||||||||
LS refinement shell | *PLUS Highest resolution: 1.55 Å / Lowest resolution: 1.58 Å |