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- PDB-1tpo: THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tpo | ||||||
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Title | THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS | ||||||
![]() | BETA-TRYPSIN | ||||||
![]() | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Bode, W. / Walter, J. / Huber, R. | ||||||
![]() | 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. #1: ![]() 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. #2: ![]() 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. #3: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 52.4 KB | Display | ![]() |
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PDB format | ![]() | 37.6 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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1 |
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Unit cell |
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Atom site foot note | 1: SEE REMARK 4. |
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Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.16 % |
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Crystal grow![]() | *PLUS Method: unknown |
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Processing
Refinement | Resolution: 1.7→7 Å / Rfactor Rwork![]() | ||||||||||||
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Refinement step | Cycle: LAST / Resolution: 1.7→7 Å
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