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- PDB-4c2g: Crystal structure of CtpB(S309A) in complex with a peptide having... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4c2g | ||||||
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Title | Crystal structure of CtpB(S309A) in complex with a peptide having a Val-Pro-Ala C-terminus | ||||||
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![]() | HYDROLASE/PEPTIDE / HYDROLASE-PEPTIDE COMPLEX / 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 | ![]() | 109.3 KB | Display | ![]() |
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PDB format | ![]() | 81.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.8 KB | Display | ![]() |
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Full document | ![]() | 441.3 KB | Display | |
Data in XML | ![]() | 21.4 KB | Display | |
Data in CIF | ![]() | 31.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4c2cSC ![]() 4c2dC ![]() 4c2eC ![]() 4c2fC ![]() 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 49724.480 Da / Num. of mol.: 1 / Fragment: RESIDUES 46-478 / 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: 302.326 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: 1258.419 Da / Num. of mol.: 1 / Fragment: RESIDUES 29-40 / Source method: obtained synthetically / Details: PEPTIDE NH2-EMDKPQTAAVPA-COOH Source: (synth.) ![]() ![]() References: UniProt: O35002, C-terminal processing peptidase |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.14 % / 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: DECTRIS PILATUS 6M / Detector: PIXEL |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→102.81 Å / Num. obs: 45714 / % possible obs: 98.5 % / Observed criterion σ(I): -10 / Redundancy: 3.2 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 23.4 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.7 / Mean I/σ(I) obs: 1.8 / % possible all: 97.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4C2C Resolution: 1.9→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: 54.385 Å2 / ksol: 0.36 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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