[English] 日本語
![](img/lk-miru.gif)
- PDB-1fle: CRYSTAL STRUCTURE OF ELAFIN COMPLEXED WITH PORCINE PANCREATIC ELASTASE -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1fle | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF ELAFIN COMPLEXED WITH PORCINE PANCREATIC ELASTASE | ||||||
![]() |
| ||||||
![]() | COMPLEX (SERINE PROTEASE/INHIBITOR) / HYDROLASE / SERINE PROTEASE / ZYMOGEN / PANCREAS / COMPLEX (SERINE PROTEASE-INHIBITOR) / COMPLEX (SERINE PROTEASE-INHIBITOR) complex | ||||||
Function / homology | ![]() structural constituent of skin epidermis / copulation / pancreatic elastase / Formation of the cornified envelope / peptide cross-linking / cornified envelope / Antimicrobial peptides / endopeptidase inhibitor activity / extracellular matrix / serine-type endopeptidase inhibitor activity ...structural constituent of skin epidermis / copulation / pancreatic elastase / Formation of the cornified envelope / peptide cross-linking / cornified envelope / Antimicrobial peptides / endopeptidase inhibitor activity / extracellular matrix / serine-type endopeptidase inhibitor activity / antibacterial humoral response / serine-type endopeptidase activity / innate immune response / proteolysis / extracellular space / extracellular region / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Tsunemi, M. / Matsuura, Y. / Sakakibara, S. / Katsube, Y. | ||||||
![]() | ![]() Title: Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 A resolution. Authors: Tsunemi, M. / Matsuura, Y. / Sakakibara, S. / Katsube, Y. #1: ![]() Title: Crystallization of a Complex between an Elastase-Specific Inhibitor Elafin and Porcine Pancreatic Elastase Authors: Tsunemi, M. / Matsuura, Y. / Sakakibara, S. / Katsube, Y. #2: ![]() Title: Synthesis and Structure-Activity Relationships of Elafin, an Elastase-Specific Inhibitor Authors: Tsunemi, M. / Kato, H. / Nishiuchi, Y. / Kumagaye, S. / Sakakibara, S. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 70.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 51.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 377.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 393.9 KB | Display | |
Data in XML | ![]() | 9.2 KB | Display | |
Data in CIF | ![]() | 13.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 25928.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
---|---|
#2: Protein | Mass: 6014.225 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40 % | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 5.9 / Details: pH 5.9 | |||||||||||||||
Crystal | *PLUS | |||||||||||||||
Crystal grow | *PLUS Method: macroseeding | |||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 293 K |
---|---|
Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Dec 1, 1992 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 15809 / % possible obs: 76.8 % / Observed criterion σ(I): 1 / Redundancy: 1.7 % / Rmerge(I) obs: 0.058 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. measured all: 20575 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 1.9→10 Å / σ(F): 1
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.81 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.21 Å / Luzzati d res low obs: 10 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 15659 / Rfactor obs: 0.197 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |