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- PDB-1d6r: CRYSTAL STRUCTURE OF CANCER CHEMOPREVENTIVE BOWMAN-BIRK INHIBITOR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1d6r | ||||||
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Title | CRYSTAL STRUCTURE OF CANCER CHEMOPREVENTIVE BOWMAN-BIRK INHIBITOR IN TERNARY COMPLEX WITH BOVINE TRYPSIN AT 2.3 A RESOLUTION. STRUCTURAL BASIS OF JANUS-FACED SERINE PROTEASE INHIBITOR SPECIFICITY | ||||||
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![]() | HYDROLASE / PROTEASE INHIBITOR / SERINE PROTEASE / BOWMAN-BIRK INHIBITOR | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase inhibitor activity / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Koepke, J. / Ermler, U. / Wenzl, G. / Flecker, P. | ||||||
![]() | ![]() Title: Crystal structure of cancer chemopreventive Bowman-Birk inhibitor in ternary complex with bovine trypsin at 2.3 A resolution. Structural basis of Janus-faced serine protease inhibitor specificity. Authors: Koepke, J. / Ermler, U. / Warkentin, E. / Wenzl, G. / Flecker, P. #1: ![]() Title: Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution-structural peculiarities in a folded protein conformation. Authors: Voss, R.H. / Ermler, U. / Essen, L.O. / Wenzl, G. / Kim, Y.M. / Flecker, P. #2: ![]() Title: Chemical synthesis, molecular cloning and expression of gene coding for a Bowman-Birk-type proteinase inhibitor Authors: Flecker, P. #3: ![]() Title: Proteolytic cleavage of soybean Bowman-Birk inhibitor monitored by means of high-performance capillary electrophoresis Authors: Jensen, B. / Unger, K.K. / Uebe, J. / Gey, M. / Kim, Y.M. / Flecker, P. #4: ![]() Title: A new and general procedure for refolding mutant Bowman-Birk-type proteinase inhibitors on trypsin-Sepharose as a matrix with complementary structure Authors: Flecker, P. #5: ![]() Title: Template-directed protein folding into a metastable state of increased activity Authors: Flecker, P. #6: ![]() Title: Mutational analysis of disulfide bonds in the trypsin-reactive subdomain of a Bowman-Birk-type inhibitor of trypsin and chymotrypsin. Cooperative versus autonomous refolding of subdomains. Authors: Philipp, S. / Kim, Y.M. / Durr, I. / Wenzl, G. / Vogt, M. / Flecker, P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.3 KB | Display | ![]() |
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PDB format | ![]() | 50.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.5 KB | Display | ![]() |
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Full document | ![]() | 432.2 KB | Display | |
Data in XML | ![]() | 14.6 KB | Display | |
Data in CIF | ![]() | 20.1 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 / Fragment: CATIONIC PRECURSOR / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 6431.538 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: Water | ChemComp-HOH / |
Compound details | TRIPLE-STRANDED B-HAIRPIN MOTIF OF BOWMAN-BIRK PROTEASE INHIBITOR INTERACTS WITH SURFACE LOOPS ...TRIPLE-STRANDED B-HAIRPIN MOTIF OF BOWMAN-BIRK PROTEASE INHIBITOR INTERACTS WITH SURFACE LOOPS SURROUNDIN |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.33 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8 Details: PROTEIN SOLUTION: TRIS/CL, CACL2, MGSO4.7H2O, NAN3 PLUS PRECIPITANT PRECIPITANTS: (NH4)2SO4, MDP, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 291.0K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / Method: microdialysis | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: WEISSENBERG / Detector: DIFFRACTOMETER / Date: Apr 5, 1994 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.04 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→10 Å / Num. all: 54604 / Num. obs: 54604 / % possible obs: 82.3 % / Observed criterion σ(F): 0.01 / Observed criterion σ(I): 0.01 / Redundancy: 4.838 % / Biso Wilson estimate: 30 Å2 / Rmerge(I) obs: 0.08 |
Reflection shell | Resolution: 2.3→2.4 Å / % possible all: 60.9 |
Reflection | *PLUS Num. obs: 18001 / Num. measured all: 54604 |
Reflection shell | *PLUS % possible obs: 60.9 % |
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Processing
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Refinement | Resolution: 2.3→8 Å / σ(F): 2 / Stereochemistry target values: ENGH & HUBER / Details: USED WEIGHTED FULL MATRIX LEAST SQUARES PROCEDURE.
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Refinement step | Cycle: LAST / Resolution: 2.3→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 8 Å / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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