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- PDB-4c2e: Crystal structure of the protease CtpB(S309A) present in a restin... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4c2e | ||||||
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Title | Crystal structure of the protease CtpB(S309A) present in a resting state | ||||||
![]() | CARBOXY-TERMINAL PROCESSING PROTEASE CTPB | ||||||
![]() | HYDROLASE / PROTEOLYTIC TUNNEL | ||||||
Function / homology | ![]() C-terminal processing peptidase / peptide metabolic process / sporulation resulting in formation of a cellular spore / peptide binding / peptidase activity / outer membrane-bounded periplasmic space / endopeptidase activity / serine-type endopeptidase activity / signal transduction / protein homodimerization activity ...C-terminal processing peptidase / peptide metabolic process / sporulation resulting in formation of a cellular spore / peptide binding / peptidase activity / outer membrane-bounded periplasmic space / 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 | ![]() | 199.8 KB | Display | ![]() |
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PDB format | ![]() | 158 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.3 KB | Display | ![]() |
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Full document | ![]() | 440 KB | Display | |
Data in XML | ![]() | 41.5 KB | Display | |
Data in CIF | ![]() | 63.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4c2cSC ![]() 4c2dC ![]() 4c2fC ![]() 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: 49768.535 Da / Num. of mol.: 2 / 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 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.55 % / Description: NONE |
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Crystal grow | Details: 10% ISOPROPANOL, 0.1 M IMIDAZOL PH 8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / 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: 1.8→46.28 Å / Num. obs: 93531 / % possible obs: 96.7 % / Observed criterion σ(I): -10 / Redundancy: 3.9 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 17.8 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 3.6 / % possible all: 95.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4C2C Resolution: 1.8→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: 57.5397 Å2 / ksol: 0.37 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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