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- PDB-2sbt: A COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF SUBTILISIN BP... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2sbt | ||||||
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Title | A COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF SUBTILISIN BPN AND SUBTILISIN NOVO | ||||||
![]() | SUBTILISIN NOVO | ||||||
![]() | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | ![]() subtilisin / sporulation resulting in formation of a cellular spore / fibrinolysis / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Drenth, J. / Hol, W.G.J. / Jansonius, J.N. / Koekoek, R. | ||||||
![]() | ![]() Title: A comparison of the three-dimensional structures of subtilisin BPN' and subtilisin novo. Authors: Drenth, J. / Hol, W.G. / Jansonius, J.N. / Koekoek, R. #1: ![]() Title: Subtilisin Novo,the Three-Dimensional Structure and its Comparison with Subtilisin Bpn Authors: Drenth, J. / Hol, W.G.J. / Jansonius, J.N. / Koekoek, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.6 KB | Display | ![]() |
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PDB format | ![]() | 35.2 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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Unit cell |
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Components
#1: Protein | Mass: 27552.525 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-ACN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 37.84 % |
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Crystal grow | *PLUS Method: otherDetails: Birktoft, J.J., (1969) Biophys. Res. Commun., 36, 131. |
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Processing
Refinement | Highest resolution: 2.8 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.8 Å
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