[English] 日本語
![](img/lk-miru.gif)
- PDB-6est: INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3(TFLA) WITH POR... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 6est | ||||||
---|---|---|---|---|---|---|---|
Title | INTERACTION OF THE PEPTIDE CF3-LEU-ALA-NH-C6H4-CF3(TFLA) WITH PORCINE PANCREATIC ELASTASE. X-RAY STUDIES AT 1.8 ANGSTROMS | ||||||
![]() | PORCINE PANCREATIC ELASTASE | ||||||
![]() | HYDROLASE(SERINE PROTEINASE) | ||||||
Function / homology | ![]() pancreatic elastase / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Prange, T. / Li De Lasierra, I. | ||||||
![]() | ![]() Title: Interaction of the peptide CF3-Leu-Ala-NH-C6H4-CF3 (TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 A. Authors: de la Sierra, I.L. / Papamichael, E. / Sakarellos, C. / Dimicoli, J.L. / Prange, T. #1: ![]() Title: The Atomic Structure of Crystalline Porcine Pancreatic Elastase at 2.5 Angstroms Resolution. Comparisons with the Structure of Alpha-Chymotrypsin Authors: Sawyer, L. / Shotton, C.M. / Campbell, J.W. / Wendell, P.L. / Muirhead, H. / Watson, H.C. / Diamond, R. / Ladner, R.C. #2: ![]() Title: The Indirect Mechanism of Action of the Trifluoroacetyl Peptides on Elastase Authors: Dimicoli, J.-L. / Renaud, A. / Bieth, J. #3: ![]() Title: Crystallographic Study of the Binding of a Tri-Fluoroacetyl Dipeptide Anilide Inhibitor with Elastase Authors: Hughes, D.L. / Diecker, L.C. / Bieth, L.C. / Dimicoli, J.-L. #4: ![]() Title: Structure of native porcine pancreatic elastase at 1.65 A resolutions. Authors: Meyer, E. / Cole, G. / Radhakrishnan, R. / Epp, O. #5: ![]() Title: Structure of the Product Complex of Acetyl-Ala-Pro-Ala with Porcine Pancreatic Elastase at 1.65 A Resolution Authors: Meyer, E. / Radhakrishnan, R. / Cole, G. / Presta, L.G. | ||||||
History |
| ||||||
Remark 700 | SHEET THE TWO SEVEN STRANDED SHEETS IN THIS STRUCTURE ARE REALLY SIX STRANDED BETA BARRELS. THIS IS ...SHEET THE TWO SEVEN STRANDED SHEETS IN THIS STRUCTURE ARE REALLY SIX STRANDED BETA BARRELS. THIS IS DENOTED BY THE FIRST STRAND RECURRING AS THE LAST STRAND. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 62.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 45.6 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: 25928.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||||
---|---|---|---|---|---|
#2: Chemical | ChemComp-CA / | ||||
#3: Chemical | ChemComp-SO4 / | ||||
#4: Chemical | #5: Water | ChemComp-HOH / | Sequence details | THE RESIDUE NUMBERING SCHEME USED FOR ELASTASE WAS CHOSEN TO MAXIMIZE HOMOLOGY WITH THE NUMBERING ...THE RESIDUE NUMBERING SCHEME USED FOR ELASTASE WAS CHOSEN TO MAXIMIZE HOMOLOGY WITH THE NUMBERING FOR CHYMOTRYPS | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.11 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 5.7 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Num. obs: 11526 / Rmerge(I) obs: 0.092 |
-
Processing
Software | Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.2 / Highest resolution: 1.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 11233 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |