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- PDB-1sel: CRYSTAL STRUCTURE OF SELENOSUBTILISIN AT 2.0-ANGSTROMS RESOLUTION -
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Open data
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Basic information
Entry | Database: PDB / ID: 1sel | |||||||||
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Title | CRYSTAL STRUCTURE OF SELENOSUBTILISIN AT 2.0-ANGSTROMS RESOLUTION | |||||||||
![]() | SELENOSUBTILISIN | |||||||||
![]() | HYDROLASE(SERINE PROTEASE) | |||||||||
Function / homology | ![]() subtilisin / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Syed, R. / Hogle, J.M. / Hilvert, D. | |||||||||
![]() | ![]() Title: Crystal structure of selenosubtilisin at 2.0-A resolution. Authors: Syed, R. / Wu, Z.P. / Hogle, J.M. / Hilvert, D. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 108 KB | Display | ![]() |
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PDB format | ![]() | 83 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 168 / 2: RESIDUE 221 IN CHAIN A IS A SELENOCYSTEINE. / 3: CIS PROLINE - PRO B 168 / 4: RESIDUE 221 IN CHAIN B IS A SELENOCYSTEINE. |
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Components
#1: Protein | Mass: 27401.158 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | ChemComp-CA / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.54 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 22.5 ℃ / pH: 8 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 40 Å |
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Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.13 Å / Num. possible: 2636 / Num. unique obs: 5618 / Rmerge(I) obs: 0.243 |
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Processing
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Refinement | Resolution: 2→8 Å / Rfactor Rwork: 0.173 / Rfactor obs: 0.173 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 8 Å / Num. reflection obs: 22155 / σ(I): 2 / Rfactor obs: 0.173 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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