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Yorodumi- PDB-3tpi: THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3tpi | |||||||||
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Title | THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS | |||||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / COMPLEX (PROTEINASE-INHIBITOR) / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | |||||||||
Function / homology | Function and homology information trypsinogen activation / negative regulation of serine-type endopeptidase activity / sulfate binding / potassium channel inhibitor activity / negative regulation of platelet aggregation / 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 / potassium channel inhibitor activity / negative regulation of platelet aggregation / 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 | Bos taurus (cattle) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | |||||||||
Authors | Huber, R. / Bode, W. / Deisenhofer, J. / Schwager, P. | |||||||||
Citation | 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: Journal: J.Mol.Biol. / Year: 1979 Title: The Transition of Bovine Trypsinogen to a Trypsin-Like State Upon Strong Ligand Binding. II. The Binding of the Pancreatic Trypsin Inhibitor and of Isoleucine-Valine and of Sequentially ...Title: The Transition of Bovine Trypsinogen to a Trypsin-Like State Upon Strong Ligand Binding. II. The Binding of the Pancreatic Trypsin Inhibitor and of Isoleucine-Valine and of Sequentially Related Peptides to Trypsinogen and to P-Guanidinobenzoate-Trypsinogen Authors: Bode, W. #2: Journal: J.Mol.Biol. / Year: 1978 Title: The Transition of Bovine Trypsinogen to a Trypsin-Like State Upon Strong Ligand Binding. The Refined Crystal Structures of the Bovine Trypsinogen-Pancreatic Trypsin Inhibitor Complex and of ...Title: The Transition of Bovine Trypsinogen to a Trypsin-Like State Upon Strong Ligand Binding. The Refined Crystal Structures of the Bovine Trypsinogen-Pancreatic Trypsin Inhibitor Complex and of its Ternary Complex with Ile-Val at 1.9 Angstroms Resolution Authors: Bode, W. / Schwager, P. / Huber, R. #3: Journal: Acc.Chem.Res. / Year: 1978 Title: Structural Basis of the Activation and Action of Trypsin Authors: Huber, R. / Bode, W. #4: Journal: Biophys.Struct.Mech. / Year: 1975 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. #5: Journal: J.Mol.Biol. / Year: 1974 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. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3tpi.cif.gz | 63 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3tpi.ent.gz | 51.1 KB | Display | PDB format |
PDBx/mmJSON format | 3tpi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tp/3tpi ftp://data.pdbj.org/pub/pdb/validation_reports/tp/3tpi | 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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2 |
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3 |
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4 |
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Unit cell |
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Atom site foot note | 1: SEE REMARK 4. | ||||||||
Components on special symmetry positions |
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-Components
-Protein , 2 types, 2 molecules ZI
#1: Protein | Mass: 24012.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Organ: PANCREAS / References: UniProt: P00760, trypsin |
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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 |
-Non-polymers , 5 types, 157 molecules
#3: Chemical | ChemComp-ILE / | ||
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#4: Chemical | ChemComp-VAL / | ||
#5: Chemical | ChemComp-CA / | ||
#6: Chemical | #7: Water | ChemComp-HOH / | |
-Details
Nonpolymer details | THE RESIDUES 1016 AND 1017 REPRESENT A DIPEPTIDE (ILE-VAL) BOUND TO THE ENZYME THE 229 AMINO ACIDS ...THE RESIDUES 1016 AND 1017 REPRESENT A DIPEPTIDE (ILE-VAL) BOUND TO THE ENZYME THE 229 AMINO ACIDS OF TRYPSINOGE |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.18 Å3/Da / Density % sol: 61.32 % |
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Crystal grow | *PLUS Method: unknown |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Refinement | Resolution: 1.9→6.8 Å / Rfactor Rwork: 0.193 | ||||||||||||
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Refinement step | Cycle: LAST / Resolution: 1.9→6.8 Å
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