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- PDB-1ton: RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE SOLUTION... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ton | ||||||
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Title | RAT SUBMAXILLARY GLAND SERINE PROTEASE, TONIN. STRUCTURE SOLUTION AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION | ||||||
![]() | TONIN | ||||||
![]() | HYDROLASE(SERINE PROTEINASE) | ||||||
Function / homology | ![]() tissue kallikrein / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Activation of Matrix Metalloproteinases / regulation of systemic arterial blood pressure / zymogen activation / serine-type peptidase activity / secretory granule / serine-type endopeptidase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Fujinaga, M. / James, M.N.G. | ||||||
![]() | ![]() Title: Rat submaxillary gland serine protease, tonin. Structure solution and refinement at 1.8 A resolution. Authors: Fujinaga, M. / James, M.N. #1: ![]() Title: Kallikrein-Related M/Rnas of the Rat Submaxillary Gland. Nucleotide Sequences of Four Distinct Types Including Tonin Authors: Ashley, P.L. / Macdonald, R.J. #2: ![]() Title: Amino Acid Sequence of Rat Submaxillary Tonin Reveals Similarities to Serine Proteases Authors: Lazure, C. / Leduc, R. / Seidah, N.G. / Thibault, G. / Genest, J. / Chretien, M. #3: ![]() Title: Crystal Data for Tonin, an Enzyme Involved in the Formation of Angiotensin II Authors: Hayakawa, K. / Kelly, J.A. / James, M.N.G. | ||||||
History |
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Remark 650 | HELIX THE SECONDARY STRUCTURE SPECIFICATIONS PRESENTED ON THE *HELIX* AND *TURN* RECORDS BELOW WERE ...HELIX THE SECONDARY STRUCTURE SPECIFICATIONS PRESENTED ON THE *HELIX* AND *TURN* RECORDS BELOW WERE EXTRACTED FROM THE PUBLICATION CITED ON THE *JRNL* RECORDS ABOVE. THIS INFORMATION WAS GENERATED USING THE PROCEDURE DEFINED BY W. KABSCH AND C. SANDER (BIOPOLYMERS, V. 22, P. 2577, 1983). | ||||||
Remark 700 | SHEET SHEETS *S1A* AND *S1B* FORM A SANDWICH. SHEETS *S2A* AND *S2B* FORM A SANDWICH. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 55.5 KB | Display | ![]() |
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PDB format | ![]() | 43.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.4 KB | Display | ![]() |
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Full document | ![]() | 374.4 KB | Display | |
Data in XML | ![]() | 6.9 KB | Display | |
Data in CIF | ![]() | 10.6 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: RESIDUE 219 IS A CIS PROLINE. / 2: SEE REMARK 4. |
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Components
#1: Protein | Mass: 25686.357 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Water | ChemComp-HOH / |
Nonpolymer details | THE ZINC ION IS ALSO BONDED TO OE2 GLU 148 OF A SYMMETRY-RELATED MOLECULE. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.47 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Biso Wilson estimate: 16.1 Å2 |
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Reflection shell | *PLUS |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||
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Refinement | Resolution: 1.8→8 Å / Rfactor obs: 0.196 / σ(I): 0 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
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Refinement | *PLUS σ(I): 1 / Highest resolution: 1.8 Å / Lowest resolution: 8 Å / Num. reflection obs: 14997 / Rfactor obs: 0.196 | ||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||
Refine LS restraints | *PLUS
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