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- PDB-1bpt: CREVICE-FORMING MUTANTS OF BPTI: CRYSTAL STRUCTURES OF F22A, Y23A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bpt | ||||||
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Title | CREVICE-FORMING MUTANTS OF BPTI: CRYSTAL STRUCTURES OF F22A, Y23A, N43G, AND F45A | ||||||
![]() | BOVINE PANCREATIC TRYPSIN INHIBITOR | ||||||
![]() | PROTEINASE INHIBITOR (TRYPSIN) | ||||||
Function / homology | ![]() 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 / serine protease inhibitor complex / serine-type endopeptidase inhibitor activity ...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 / serine protease inhibitor complex / serine-type endopeptidase inhibitor activity / protease binding / calcium ion binding / extracellular space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Housset, D. / Wlodawer, A. / Tao, F. / Fuchs, J. / Woodward, C. | ||||||
![]() | ![]() Title: Crevice-forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: crystal structures of F22A, Y23A, N43G, and F45A. Authors: Danishefsky, A.T. / Housset, D. / Kim, K.S. / Tao, F. / Fuchs, J. / Woodward, C. / Wlodawer, A. #1: ![]() Title: Crevice-Forming Mutants of Bpti: Stability Changes and New Hydrophobic Surface Authors: Kim, K.S. / Tao, F. / Fuchs, J. / Danishefsky, A.T. / Housset, D. / Wlodawer, A. / Woodward, C. #2: ![]() Title: Crystal Structure of a Y35G Mutant of Bovine Pancreatic Trypsin Inhibitor Authors: Housset, D. / Kim, K.-S. / Fuchs, J. / Woodward, C. / Wlodawer, A. #3: ![]() Title: Structural Effects Induced by Removal of a Disulfide-Bridge. The X-Ray Structure of the C30A(Slash)C51A Mutant of Basic Pancreatic Trypsin Inhibitor at 1.6 Angstroms Authors: Eigenbrot, C. / Randal, M. / Kossiakoff, A.A. #4: ![]() Title: X-Ray Crystal Structure of the Protease Inhibitor Domain of Alzheimer'S Amyloid Beta-Protein Precursor Authors: Hynes, T.R. / Randal, M. / Kennedy, L.A. / Eigenbrot, C. / Kossiakoff, A.A. #5: ![]() Title: Structure of Form III Crystals of Bovine Pancreatic Trypsin Inhibitor. Authors: Wlodawer, A. / Nachman, J. / Gilliland, G.L. / Woodward, W.Gallagher C. #6: ![]() Title: Structure of Bovine Pancreatic Trypsin Inhibitor. Results of Joint Neutron and X-Ray Refinement of Crystal Form II Authors: Wlodawer, A. / Walter, J. / Huber, R. / Sjolin, L. #7: ![]() Title: Comparison of Two Highly Refined Structures of Bovine Pancreatic Trypsin Inhibitor Authors: Wlodawer, A. / Deisenhofer, J. / Huber, R. #8: ![]() Title: Pancreatic Trypsin Inhibitor. A New Crystal Form and its Analysis Authors: Walter, J. / Huber, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 23.5 KB | Display | ![]() |
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PDB format | ![]() | 14.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 6435.472 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-PO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.84 Å3/Da / Density % sol: 33.07 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 9.7 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
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: 1.98 Å / Lowest resolution: 10 Å / Num. obs: 2996 / % possible obs: 88 % / Rmerge(I) obs: 0.085 |
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Processing
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Refinement | Rfactor Rwork: 0.165 / Highest resolution: 2 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints | Type: x_bond_d / Dev ideal: 0.018 | ||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||
Refinement | *PLUS Rfactor obs: 0.165 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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