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- PDB-1slv: RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1slv | ||||||
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Title | RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND | ||||||
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![]() | COMPLEX (SERINE PROTEASE/INHIBITOR) / SERINE PROTEASE / INHIBITOR / COMPLEX / METAL BINDING SITES / PROTEIN ENGINEERING / PROTEASE-SUBSTRATE INTERACTIONS / METALLOPROTEINS / COMPLEX (SERINE PROTEASE-INHIBITOR) COMPLEX | ||||||
Function / homology | ![]() Antimicrobial peptides / Alpha-defensins / Activation of Matrix Metalloproteinases / Neutrophil degranulation / collagen catabolic process / trypsin / digestion / response to nutrient / serine-type endopeptidase inhibitor activity / outer membrane-bounded periplasmic space ...Antimicrobial peptides / Alpha-defensins / Activation of Matrix Metalloproteinases / Neutrophil degranulation / collagen catabolic process / trypsin / digestion / response to nutrient / serine-type endopeptidase inhibitor activity / outer membrane-bounded periplasmic space / serine-type endopeptidase activity / calcium ion binding / protein homodimerization activity / proteolysis / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Brinen, L.S. / Fletterick, R.J. | ||||||
![]() | ![]() Title: X-ray structures of a designed binding site in trypsin show metal-dependent geometry. Authors: Brinen, L.S. / Willett, W.S. / Craik, C.S. / Fletterick, R.J. #1: ![]() Title: Macromolecular Chelation as an Improved Mechanism of Protease Inhibition: Structure of the Ecotin-Trypsin Complex Authors: Mcgrath, M.E. / Erpel, T. / Bystroff, C. / Fletterick, R.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.4 KB | Display | ![]() |
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PDB format | ![]() | 62.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 384.1 KB | Display | ![]() |
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Full document | ![]() | 389.5 KB | Display | |
Data in XML | ![]() | 8.8 KB | Display | |
Data in CIF | ![]() | 13 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 16187.577 Da / Num. of mol.: 1 / Mutation: CHAIN A, A86H Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 23847.914 Da / Num. of mol.: 1 / Mutation: CHAIN B, N143H, E151H Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 4 types, 69 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/CU.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/CU.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-CA / |
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#4: Chemical | ChemComp-ACT / |
#5: Chemical | ChemComp-CU / |
#6: Water | ChemComp-HOH / |
-Details
Compound details | SITE DIRECTED MUTAGENESIS WAS PERFORMED IN ORDER TO DESIGN A METAL BINDING SITE AT THE INTERFACE OF ...SITE DIRECTED MUTAGENESI |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.39 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Jun 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 16190 / % possible obs: 96.1 % / Observed criterion σ(I): 1.5 / Redundancy: 3 % / Rmerge(I) obs: 0.064 |
Reflection | *PLUS Num. measured all: 58971 |
Reflection shell | *PLUS % possible obs: 92.7 % |
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Processing
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Refinement | Resolution: 2.3→6 Å / σ(F): 1.5
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Displacement parameters | Biso mean: 34.19 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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