+
Open data
-
Basic information
Entry | Database: PDB / ID: 1fn6 | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.1% POLYDOCANOL | ||||||
![]() | TRYPSIN | ||||||
![]() | HYDROLASE / SERINE PROTEASE | ||||||
Function / homology | ![]() trypsin / digestion / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Deepthi, S. / Johnson, A. / Pattabhi, V. | ||||||
![]() | ![]() Title: Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol. Authors: Deepthi, S. / Johnson, A. / Pattabhi, V. #1: ![]() Title: Crystal Structure at 1.63 Angstroms Resolution of the Native Form of Porcine Beta Trypsin : Revealing an Acetate Ion Binding Site and Functional Water Network Authors: Johnson, A. / Gautham, N. / Pattabhi, V. #2: ![]() Title: The First Structure at 1.8 Angstroms Resolution of an Active Autolysate Form of Porcine Alpha Trypsin Authors: Johnson, A. / Krishnaswamy, S. / Sundaram, P.V. / Pattabhi, V. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 60.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 42.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 392.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 396.5 KB | Display | |
Data in XML | ![]() | 7 KB | Display | |
Data in CIF | ![]() | 10.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fmgC ![]() 1fniC ![]() 1qquS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 23491.525 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|
-Non-polymers , 5 types, 161 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/MOH.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/EDO.gif)
![](data/chem/img/MOH.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CA / | ||||
---|---|---|---|---|---|
#3: Chemical | ChemComp-SO4 / | ||||
#4: Chemical | #5: Chemical | ChemComp-MOH / | #6: Water | ChemComp-HOH / | |
-Details
Sequence details | THE 223 AMINO ACIDS OF TRYPSIN ARE IDENTIFIED |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.86 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Method: vapor diffusion, hanging drop / pH: 6.7 / Details: pH 6.70, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K / pH: 6.7 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 293 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 16, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→26.26 Å / Num. obs: 17686 / % possible obs: 92.63 % / Observed criterion σ(I): 0 / Redundancy: 3.84 % / Rmerge(I) obs: 0.0677 / Net I/σ(I): 14.61 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.4495 / Mean I/σ(I) obs: 1.35 / % possible all: 88.4 |
Reflection | *PLUS Num. measured all: 67986 |
Reflection shell | *PLUS Num. unique obs: 4514 / Rmerge(I) obs: 0.361 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 1QQU Resolution: 1.8→8 Å / Cross valid method: FREE R / σ(F): 0
| ||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
| ||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR,REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.8 Å / % reflection Rfree: 4.85 % / Rfactor all: 0.162 / Rfactor obs: 0.157 / Rfactor Rfree: 0.238 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|