+Open data
-Basic information
Entry | Database: PDB / ID: 1sua | ||||||
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Title | SUBTILISIN BPN' | ||||||
Components |
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Keywords | COMPLEX (HYDROLASE/PEPTIDE) / COMPLEX (HYDROLASE-PEPTIDE) / HYDROLASE / SERINE PROTEINASE / COMPLEX (HYDROLASE-PEPTIDE) complex | ||||||
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 / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Almog, O. / Gilliland, G.L. | ||||||
Citation | Journal: Proteins / Year: 1998 Title: Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain. Authors: Almog, O. / Gallagher, T. / Tordova, M. / Hoskins, J. / 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 | 1sua.cif.gz | 58.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1sua.ent.gz | 44.9 KB | Display | PDB format |
PDBx/mmJSON format | 1sua.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/su/1sua ftp://data.pdbj.org/pub/pdb/validation_reports/su/1sua | HTTPS FTP |
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-Related structure data
Related structure data | 1sucS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 26622.480 Da / Num. of mol.: 1 Mutation: DEL(75-83), K43N, M50F, G73A, Q206V, Y217K, N218S, S221A, Q271E Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Cell line: BL21 / Cellular location: EXTRACELLULARGlossary of biology / Plasmid: BL21 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P00782, subtilisin |
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#2: Protein/peptide | Mass: 386.486 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source |
#3: Water | ChemComp-HOH / |
Compound details | GLN 275 IS THE LAST RESIDUE BEFORE THE TETRA PEPTIDE ALAL. ALAL IS IN THE ACTIVE SITE. |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: 1.25M LI2SO4 0.1M HEPES/HCL PH7.5 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jul 1, 1994 |
Radiation | Monochromator: NI/FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.1 Å / Num. obs: 13358 / % possible obs: 82 % / Redundancy: 3 % / Rsym value: 0.123 / Net I/σ(I): 6 |
Reflection shell | Resolution: 2.1→2.19 Å / Redundancy: 0.5 % / Mean I/σ(I) obs: 1 / Rsym value: 0.37 / % possible all: 34 |
Reflection | *PLUS Observed criterion σ(I): 1 / Num. measured all: 39158 / Rmerge(I) obs: 0.12 |
Reflection shell | *PLUS Lowest resolution: 2.2 Å / % possible obs: 91 % / Rmerge(I) obs: 0.37 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1SUC Resolution: 2.1→8 Å / σ(F): 2
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Displacement parameters | Biso mean: 10.36 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→8 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |