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- PDB-1tgs: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN PANCREATIC SEC... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tgs | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN PANCREATIC SECRETORY INHIBITOR (KAZAL TYPE) AND TRYPSINOGEN AT 1.8 ANGSTROMS RESOLUTION. STRUCTURE SOLUTION, CRYSTALLOGRAPHIC REFINEMENT AND PRELIMINARY STRUCTURAL INTERPRETATION | ||||||
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![]() | COMPLEX (PROTEINASE/INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) complex | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Bolognesi, M. / Gatti, G. / Menegatti, E. / Guarneri, M. / Marquart, M. / Papamokos, E. / Huber, R. | ||||||
![]() | ![]() Title: Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and ...Title: Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation. Authors: Bolognesi, M. / Gatti, G. / Menagatti, E. / Guarneri, M. / Marquart, M. / Papamokos, E. / Huber, R. #1: ![]() 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.5 KB | Display | ![]() |
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PDB format | ![]() | 47.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.4 KB | Display | ![]() |
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Full document | ![]() | 440 KB | Display | |
Data in XML | ![]() | 14.5 KB | Display | |
Data in CIF | ![]() | 20.3 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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Unit cell |
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Atom site foot note | 1: SEE REMARK 4. |
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Components
#1: Protein | Mass: 24012.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 6028.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#3: Chemical | ChemComp-SO4 / |
#4: Chemical | ChemComp-CA / |
#5: Water | ChemComp-HOH / |
Sequence details | THE 229 AMINO ACIDS OF TRYPSINOGEN ARE IDENTIFIED BY THE RESIDUE NUMBERS OF THE HOMOLOGOUS ...THE 229 AMINO ACIDS OF TRYPSINOGE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.37 % |
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Crystal grow | *PLUS Method: other / Details: Bolognesi, M., (1981) J. Mol. Biol., 145, 603. |
-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 26341 / % possible obs: 84 % / Rmerge(I) obs: 0.084 |
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Processing
Refinement | Resolution: 1.8→7 Å / Rfactor Rwork: 0.186 | ||||||||||||
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Refinement step | Cycle: LAST / Resolution: 1.8→7 Å
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Refinement | *PLUS Num. reflection obs: 26341 / Rfactor obs: 0.195 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |