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Open data
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Basic information
Entry | Database: PDB / ID: 4c2h | ||||||
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Title | Crystal structure of the CtpB(V118Y) mutant | ||||||
![]() | CARBOXY-TERMINAL PROCESSING PROTEASE CTPB | ||||||
![]() | HYDROLASE / PDZ-PROTEASES / ALLOSTERIC REGULATION / CONFORMATIONAL SWITCH / SPORULATION / 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 | ![]() | 188.8 KB | Display | ![]() |
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PDB format | ![]() | 149.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.6 KB | Display | ![]() |
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Full document | ![]() | 452.6 KB | Display | |
Data in XML | ![]() | 37.4 KB | Display | |
Data in CIF | ![]() | 54.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4c2cSC ![]() 4c2dC ![]() 4c2eC ![]() 4c2fC ![]() 4c2gC 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: 49848.578 Da / Num. of mol.: 2 / Fragment: RESIDUES 44-478 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() 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: 2.56 Å3/Da / Density % sol: 52.03 % / Description: NONE |
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Crystal grow | Details: 15% 2-METHYL-2,4-PENTANEDIOL, 5% PEG 4000, 0.1M IMIDAZOLE PH 8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / 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: 1.95→46.1 Å / Num. obs: 67539 / % possible obs: 93.9 % / Observed criterion σ(I): -10 / Redundancy: 2.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 8.3 |
Reflection shell | Resolution: 1.95→2.06 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 1.8 / % possible all: 84.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4C2C Resolution: 1.95→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: 68.7393 Å2 / ksol: 0.4 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.95→20 Å
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Refine LS restraints |
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