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- PDB-1s01: LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) TH... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1s01 | |||||||||
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Title | LARGE INCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING | |||||||||
![]() | Subtilisin BPN' | |||||||||
![]() | HYDROLASE / 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 | ![]() | |||||||||
![]() | Whitlow, M. / Howard, A.J. / Wood, J.F. | |||||||||
![]() | ![]() Title: Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Authors: Pantoliano, M.W. / Whitlow, M. / Wood, J.F. / Dodd, S.W. / Hardman, K.D. / Rollence, M.L. / Bryan, P.N. #1: ![]() Title: Enzymes in Organic Synthesis. Use of Subtilisin and a Highly Stable Mutant Derived from Multiple Site-Specific Mutations Authors: Wong, C.-H. / Chen, S.-T. / Hennen, W.J. / Bibbs, J.A. / Wang, Y.-F. / Liu, J.L.-C. / Pantoliano, M.W. / Whitlow, M. / Bryan, P.N. #2: ![]() Title: The Engineering of Binding Affinity at Metal Ion Binding Sites for the Stabilization of Proteins. Subtilisin as a Test Case Authors: Pantoliano, M.W. / Whitlow, M. / Wood, J.F. / Rollence, M.L. / Finzel, B.C. / Gilliland, G.L. / Poulos, T.L. / Bryan, P.N. #3: ![]() Title: Engineering Thermostability in Subtilisin Bpn(Prime) by in Vitro Mutagenesis Authors: Rollence, M.L. / Filpula, D. / Pantoliano, M.W. / Bryan, P.N. #4: ![]() Title: Proteases of Enhanced Stability. Characterization of a Thermostable Variant of Subtilisin Authors: Bryan, P.N. / Rollence, M.L. / Pantoiano, M.W. / Wood, J. / Finzel, B.C. / Gilliland, G.L. / Howard, A.J. / Poulos, T.L. #5: ![]() Title: Atomic Coordinates for Subtilisin Bpn(or Novo) Authors: Alden, R.A. / Birktoft, J.J. / Kraut, J. / Robertus, J.D. / Wright, C.S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 63.9 KB | Display | ![]() |
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PDB format | ![]() | 49.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Atom site foot note | 1: RESIDUE PRO 168 IS A CIS PROLINE. 2: RESIDUE 206 APPEARS TO BE CYSTEINE PERSULFIDE. ELECTRON DENSITY FOUND BEYOND THE PERSULFIDE HAS BEEN MODELLED AS A PARTIALLY OCCUPIED CARBON ATOM. THE ADDITIONAL SULFUR AND CARBON ARE PRESENTED ON ...2: RESIDUE 206 APPEARS TO BE CYSTEINE PERSULFIDE. ELECTRON DENSITY FOUND BEYOND THE PERSULFIDE HAS BEEN MODELLED AS A PARTIALLY OCCUPIED CARBON ATOM. THE ADDITIONAL SULFUR AND CARBON ARE PRESENTED ON *HETATM* RECORDS AS HET GROUP * CS*. THE EXACT CHEMICAL IDENTITY OF THIS GROUP IS, HOWEVER, UNKNOWN. SEE THE PAPER CITED ON THE *JRNL* RECORDS ABOVE. |
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Components
#1: Protein | Mass: 27543.602 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-CA / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Compound details | RESIDUE 206 APPEARS TO BE CYSTEINE PERSULFIDE. ELECTRON DENSITY FOUND BEYOND THE PERSULFIDE HAS ...RESIDUE 206 APPEARS TO BE CYSTEINE PERSULFIDE | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.65 % |
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop |
Components of the solutions | *PLUS Conc.: 55 % / Common name: acetone |
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Processing
Software | Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.7→10 Å /
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Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 10 Å / Num. reflection obs: 17421 / Rfactor obs: 0.152 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |