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- PDB-1tpa: 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: 1tpa | ||||||
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Title | THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS | ||||||
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![]() | COMPLEX (PROTEINASE/INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) complex | ||||||
Function / homology | ![]() trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / trypsin / serpin family protein binding ...trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / negative regulation of platelet aggregation / potassium channel inhibitor activity / zymogen binding / molecular function inhibitor activity / negative regulation of thrombin-activated receptor signaling pathway / trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / protease binding / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Huber, R. / Bode, W. / Deisenhofer, J. | ||||||
![]() | 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 Structure of the Complex Formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. III. Structure of the Anhydro-Trypsin-Inhibitor Complex Authors: Huber, R. / Bode, W. / Kukla, D. / Kohl, U. / Ryan, C.A. #3: ![]() Title: The Single Calcium-Binding Site of Crystalline Bovine Beta-Trypsin Authors: Bode, W. / Schwager, P. #4: ![]() Title: Structure of the Complex Formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. Refinement of the Crystal Structure Analysis Authors: Huber, R. / Kukla, D. / Steigemann, W. / Deisenhofer, J. / Jones, A. #5: ![]() Title: Structure of the Complex Formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. II. Crystallographic Refinement at 1.9 Angstroms Resolution Authors: Huber, R. / Kukla, D. / Bode, W. / Schwager, P. / Bartels, K. / Deisenhofer, J. / Steigemann, W. #6: ![]() Title: Structure of the Complex Formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. Crystal Structure Determination and Stereochemistry of the Contact Region Authors: Ruehlmann, A. / Kukla, D. / Schwager, P. / Bartels, K. / Huber, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 65.6 KB | Display | ![]() |
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PDB format | ![]() | 48.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.8 KB | Display | ![]() |
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Full document | ![]() | 432.7 KB | Display | |
Data in XML | ![]() | 14.8 KB | Display | |
Data in CIF | ![]() | 20.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Atom site foot note | 1: SEE REMARK 4. / 2: SEE REMARK 6. | ||||||||
Components on special symmetry positions |
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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: Protein | Mass: 6527.568 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P00974 |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
Sequence details | RESIDUE SER E 195 HAS BEEN HYDROLYZED IN THIS MOLECULE, CONVERTING IT TO DEHYDROALANINE. TO ...RESIDUE SER E 195 HAS BEEN HYDROLYZED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.28 Å3/Da / Density % sol: 62.48 % |
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Crystal grow | *PLUS Method: unknown |
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Processing
Refinement | Resolution: 1.9→6.8 Å / Rfactor Rwork: 0.175 | ||||||||||||
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Refinement step | Cycle: LAST / Resolution: 1.9→6.8 Å
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