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- PDB-4c2f: Crystal structure of the CtpB R168A mutant present in an active c... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4c2f | ||||||
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Title | Crystal structure of the CtpB R168A mutant present in an active conformation | ||||||
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![]() | HYDROLASE / PROTEOLYTIC TUNNEL | ||||||
Function / homology | ![]() C-terminal processing peptidase / peptide metabolic process / sporulation resulting in formation of a cellular spore / peptide binding / peptidase activity / endopeptidase activity / serine-type endopeptidase activity / signal transduction / protein homodimerization activity / proteolysis / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mastny, M. / Heuck, A. / Kurzbauer, R. / Clausen, T. | ||||||
![]() | ![]() Title: Ctpb Assembles a Gated Protease Tunnel Regulating Cell-Cell Signaling During Spore Formation in Bacillus Subtilis. Authors: Mastny, M. / Heuck, A. / Kurzbauer, R. / Heiduk, A. / Boisguerin, P. / Volkmer, R. / Ehrmann, M. / Rodrigues, C.D.A. / Rudner, D.Z. / Clausen, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 101.4 KB | Display | ![]() |
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PDB format | ![]() | 77.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4c2cSC ![]() 4c2dC ![]() 4c2eC ![]() 4c2gC ![]() 4c2hC S: Starting model for refinement C: citing same article ( |
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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: 50170.207 Da / Num. of mol.: 1 / Fragment: RESIDUES 44-480 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PET21 / Production host: ![]() ![]() References: UniProt: O35002, C-terminal processing peptidase |
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#2: Protein/peptide | Mass: 231.249 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: PEPTIDE CO-PURIFIED FROM E. COLI EXPRESSION / Source: (natural) ![]() ![]() |
#3: Protein/peptide | Mass: 531.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: PEPTIDE CO-PURIFIED FROM E. COLI EXPRESSION / Source: (natural) ![]() ![]() |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.84 Å3/Da / Density % sol: 56.67 % / Description: NONE |
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Crystal grow | Details: 2.1 M NA-MALONATE PH 7.8 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→19.66 Å / Num. obs: 22841 / % possible obs: 99.7 % / Observed criterion σ(I): -10 / Redundancy: 2.8 % / Rmerge(I) obs: 0.01 / Net I/σ(I): 44.4 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2.9 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4C2C Resolution: 2.4→20 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 86.043 Å2 / ksol: 0.38 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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