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Yorodumi- PDB-1tgs: THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN PANCREATIC SEC... -
+Open data
-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 | ||||||
Components |
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Keywords | COMPLEX (PROTEINASE/INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) / COMPLEX (PROTEINASE-INHIBITOR) complex | ||||||
Function / homology | Function and homology information cap snatching / virion component / serine-type endopeptidase inhibitor activity / hydrolase activity / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / nucleotide binding / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Bolognesi, M. / Gatti, G. / Menegatti, E. / Guarneri, M. / Marquart, M. / Papamokos, E. / Huber, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1982 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: 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tgs.cif.gz | 64.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tgs.ent.gz | 47.6 KB | Display | PDB format |
PDBx/mmJSON format | 1tgs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tgs_validation.pdf.gz | 436.4 KB | Display | wwPDB validaton report |
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Full document | 1tgs_full_validation.pdf.gz | 440 KB | Display | |
Data in XML | 1tgs_validation.xml.gz | 14.5 KB | Display | |
Data in CIF | 1tgs_validation.cif.gz | 20.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tg/1tgs ftp://data.pdbj.org/pub/pdb/validation_reports/tg/1tgs | HTTPS FTP |
-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: 24012.953 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Organ: PANCREAS / References: UniProt: P00760 |
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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.) Sus scrofa (pig) / References: UniProt: P00998 |
#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: X-RAY DIFFRACTION |
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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 |