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- PDB-7est: Interaction of the peptide CF3-LEU-ALA-NH-C6H4-CF3(TFLA) with por... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7est | ||||||
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Title | Interaction of the peptide CF3-LEU-ALA-NH-C6H4-CF3(TFLA) with porcine pancreatic elastase. X-ray studies at 1.8 Angstroms | ||||||
![]() | ELASTASE | ||||||
![]() | HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | ![]() pancreatic elastase / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Li De Lasierra, I. / Prange, T. | ||||||
![]() | ![]() 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 |
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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. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 60.9 KB | Display | ![]() |
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PDB format | ![]() | 46.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 466.7 KB | Display | ![]() |
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Full document | ![]() | 474.9 KB | Display | |
Data in XML | ![]() | 7.8 KB | Display | |
Data in CIF | ![]() | 11.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6estC ![]() 2estS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 1 molecules E
#1: Protein | Mass: 25928.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 5 types, 111 molecules ![](data/chem/img/0Z2.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/DMF.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/DMF.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-0Z2 / | ||
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#3: Chemical | ChemComp-SO4 / | ||
#4: Chemical | ChemComp-CA / | ||
#5: Chemical | ChemComp-DMF / #6: Water | ChemComp-HOH / | |
-Details
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 |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.88 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.7 / Details: 10% DMF SOLUTION BUFFERED AT PH 5.7 WITH ACETATE | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 5.7 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2 Å / Num. all: 19661 / Num. obs: 11021 / Num. measured all: 10569 / Rmerge(I) obs: 0.039 |
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Processing
Software | Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Starting model: ELASTASE COMPLEXED WITH A TRIFLUOROACETYL DIPEPTIDE INHIBITOR, (PDB ENTRY 2EST) Rfactor Rwork: 0.19 / Highest resolution: 1.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.2 Å / Rfactor all: 0.169 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2 |