+Open data
-Basic information
Entry | Database: PDB / ID: 1sud | ||||||
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Title | CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN | ||||||
Components | SUBTILISIN BPN' CRB-S3 | ||||||
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: 1.9 Å | ||||||
Authors | Gallagher, T. / Bryan, P. / Gilliland, G.L. | ||||||
Citation | Journal: Proteins / Year: 1993 Title: Calcium-independent subtilisin by design. Authors: Gallagher, T. / Bryan, P. / Gilliland, G.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1sud.cif.gz | 62.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sud.ent.gz | 48 KB | Display | PDB format |
PDBx/mmJSON format | 1sud.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/su/1sud ftp://data.pdbj.org/pub/pdb/validation_reports/su/1sud | 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 PRO 168 IS A CIS PROLINE. 2: RESIDUE CYS 221 (REPLACING THE CATALYTIC SER 221) IS OXIDIZED TO A SULFONYL (TWO OXYGENS BOUND TO SG). THESE ADDUCTS ARE INCLUDED AS *HETATM* RECORDS REFERRED TO HET BONDING. 3: RESIDUE 295 IS THE 'A' SITE CALCIUM. RESIDUE CA 296 IS THE 'B' SITE CALCIUM. RESIDUE 297 IS THE 'B' SITE MONOVALENT SUBSITE. |
-Components
#1: Protein | Mass: 27555.547 Da / Num. of mol.: 1 / Mutation: M50P,Y217K, N218S,SER221CSD Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / References: UniProt: P00782, subtilisin | ||||||||
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#2: Chemical | #3: Chemical | ChemComp-K / | #4: Chemical | ChemComp-ACN / | #5: Water | ChemComp-HOH / | Compound details | SECONDARY STRUCTURE ASSIGNMENT | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 39.22 % |
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Crystal grow | *PLUS pH: 9 / Method: vapor diffusion, hanging drop |
Components of the solutions | *PLUS Conc.: 55 % / Common name: acetone |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software | Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.9→8 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 8 Å / Num. reflection obs: 15360 / σ(F): 1 / Rfactor obs: 0.179 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |