[English] 日本語
![](img/lk-miru.gif)
- PDB-1btx: Episelection: Novel Ki ~Nanomolar Inhibitors of Serine Proteases ... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1btx | ||||||
---|---|---|---|---|---|---|---|
Title | Episelection: Novel Ki ~Nanomolar Inhibitors of Serine Proteases Selected by Binding or Chemistry on an Enzyme Surface | ||||||
![]() | BETA-TRYPSIN | ||||||
![]() | HYDROLASE/HYDROLASE INHIBITOR / TRIPEPTIDEBORONATE ETHYL ESTER INHIBITED / SERINE PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Stroud, R.M. / Katz, B.A. / Finer-Moore, J. | ||||||
![]() | ![]() Title: Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface. Authors: Katz, B.A. / Finer-Moore, J. / Mortezaei, R. / Rich, D.H. / Stroud, R.M. #1: ![]() Title: Solvent Structure in Crystals of Trypsin Determined by X-Ray and Neutron Diffraction Authors: Finer-Moore, J.S. / Kossiakoff, A. / Hurley, J.H. / Earnest, T. / Stroud, R.M. #2: ![]() Title: 1.59 Angstrom Structure of Trypsin at 120K: Comparison of Low Temperature and Room Temperature Structures Authors: Earnest, T. / Fauman, E. / Craik, C.S. / Stroud, R.M. #3: ![]() Title: Difference Fourier Refinement of the Structure of Dip-Trypsin at 1.5 Angstroms Using a Minicomputer Technique Authors: Chambers, J.L. / Stroud, R.M. #4: ![]() Title: Structure and Specific Binding of Trypsin, Comparison of Inhibited Derivatives and a Model for Substrate Binding Authors: Krieger, M. / Kay, L.M. / Stroud, R.M. #5: ![]() Title: The Crystal and Molecular Structure of Dip-Inhibited Bovine Trypsin at 2.7 Angstroms Resolution Authors: Stroud, R.M. / Kay, L.M. / Dickerson, R.E. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 74.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 60.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 24012.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|---|
#2: Chemical | ChemComp-0ZX / |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
Nonpolymer details | THE INHIBITOR WAS SYNTHESIZED AS THE PINANEDIOL DIESTER P-TOLUENESULFONATE SALT. THE ETHYL ESTER ...THE INHIBITOR WAS SYNTHESIZE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.59 % | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 8.15 / Method: vapor diffusion, hanging drop / Details: used seeding | ||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 10174 / % possible obs: 40.6 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 8 Å / Num. measured all: 15280 / Rmerge(I) obs: 0.08 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.7→8 Å / σ(F): 0 /
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.14 / Rfactor Rwork: 0.14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |