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Yorodumi- PDB-2st1: THE THREE-DIMENSIONAL STRUCTURE OF BACILLUS AMYLOLIQUEFACIENS SUB... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2st1 | ||||||
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Title | THE THREE-DIMENSIONAL STRUCTURE OF BACILLUS AMYLOLIQUEFACIENS SUBTILISIN AT 1.8 ANGSTROMS AND AN ANALYSIS OF THE STRUCTURAL CONSEQUENCES OF PEROXIDE INACTIVATION | ||||||
Components | SUBTILISIN BPN' | ||||||
Keywords | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | Function and homology information subtilisin / sporulation resulting in formation of a cellular spore / fibrinolysis / serine-type endopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | Bacillus amyloliquefaciens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Bott, R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1988 Title: The three-dimensional structure of Bacillus amyloliquefaciens subtilisin at 1.8 A and an analysis of the structural consequences of peroxide inactivation. Authors: Bott, R. / Ultsch, M. / Kossiakoff, A. / Graycar, T. / Katz, B. / Power, S. #1: Journal: Nucleic Acids Res. / Year: 1983 Title: Cloning, Sequencing and Secretion of Bacillus Amyloliquefaciens Subtilisin in Bacillus Subtilis Authors: Wells, J.A. / Ferrari, E. / Henner, D.J. / Estell, D.A. / Chen, E.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2st1.cif.gz | 64.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2st1.ent.gz | 47 KB | Display | PDB format |
PDBx/mmJSON format | 2st1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/st/2st1 ftp://data.pdbj.org/pub/pdb/validation_reports/st/2st1 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE 168 IS A CIS PROLINE. |
-Components
#1: Protein | Mass: 27552.525 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / References: UniProt: P00782, 3.4.21.14 | ||||
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#2: Chemical | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.95 Å3/Da / Density % sol: 36.93 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 15461 / Num. measured all: 15461 / Rmerge(I) obs: 0.04 |
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-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Resolution: 1.8→10 Å / Rfactor obs: 0.144 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection obs: 15433 / Highest resolution: 1.8 Å / Lowest resolution: 10 Å / Rfactor obs: 0.144 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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