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- PDB-1hpt: THREE-DIMENSIONAL STRUCTURE OF A RECOMBINANT VARIANT OF HUMAN PAN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hpt | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF A RECOMBINANT VARIANT OF HUMAN PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL TYPE) | ||||||
![]() | PANCREATIC SECRETORY TRYPSIN INHIBITOR (KAZAL TYPE) VARIANT 3 | ||||||
![]() | SERINE PROTEASE INHIBITOR | ||||||
Function / homology | ![]() negative regulation of nitric oxide mediated signal transduction / regulation of acrosome reaction / positive regulation of pancreatic juice secretion / regulation of store-operated calcium entry / negative regulation of peptidyl-tyrosine phosphorylation / negative regulation of calcium ion import / cellular response to peptide hormone stimulus / sperm capacitation / endopeptidase inhibitor activity / positive regulation of peptide hormone secretion ...negative regulation of nitric oxide mediated signal transduction / regulation of acrosome reaction / positive regulation of pancreatic juice secretion / regulation of store-operated calcium entry / negative regulation of peptidyl-tyrosine phosphorylation / negative regulation of calcium ion import / cellular response to peptide hormone stimulus / sperm capacitation / endopeptidase inhibitor activity / positive regulation of peptide hormone secretion / nitric oxide mediated signal transduction / response to nutrient levels / positive regulation of epithelial cell proliferation / serine-type endopeptidase inhibitor activity / positive regulation of cytosolic calcium ion concentration / response to ethanol / extracellular exosome Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Hecht, H.J. / Szardenings, M. / Collins, J. / Schomburg, D. | ||||||
![]() | ![]() Title: Three-dimensional structure of a recombinant variant of human pancreatic secretory trypsin inhibitor (Kazal type). Authors: Hecht, H.J. / Szardenings, M. / Collins, J. / Schomburg, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 20.2 KB | Display | ![]() |
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PDB format | ![]() | 12.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 410.2 KB | Display | ![]() |
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Full document | ![]() | 410.8 KB | Display | |
Data in XML | ![]() | 4.6 KB | Display | |
Data in CIF | ![]() | 5.6 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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Unit cell |
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Components
#1: Protein | Mass: 6347.094 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.85 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.3 / Method: unknown | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.46 Å / Num. all: 2483 / Num. obs: 4612 / Num. measured all: 2200 / Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Resolution: 2.3→8 Å / Rfactor Rwork: 0.191 / Rfactor obs: 0.191 / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.191 / Num. reflection obs: 2200 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 14.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 4 Å / Lowest resolution: 10 Å / Rfactor all: 0.466 |