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Open data
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Basic information
Entry | Database: PDB / ID: 7zhe | ||||||
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Title | Crystal structure of CtaZ from Ruminiclostridium cellulolyticum | ||||||
![]() | Transcription activator effector binding | ||||||
![]() | LIPID BINDING PROTEIN / GYRASE-LIKE DOMAIN / RECEPTOR / SIDEROPHORE / SELF PROTECTION / ANTIBIOTIC RESISTANCE / DRUG BINDING | ||||||
Function / homology | Bacterial transcription activator, effector binding / Bacterial transcription activator, effector binding domain / GyrI-like small molecule binding domain / GyrI-like small molecule binding domain / Regulatory factor, effector binding domain superfamily / Transcription activator effector binding![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gude, F. / Molloy, E.M. / Horch, T. / Dell, M. / Dunbar, K.L. / Krabbe, J. / Groll, M. / Hertweck, C. | ||||||
Funding support | European Union, 1items
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![]() | ![]() Title: A Specialized Polythioamide-Binding Protein Confers Antibiotic Self-Resistance in Anaerobic Bacteria. Authors: Gude, F. / Molloy, E.M. / Horch, T. / Dell, M. / Dunbar, K.L. / Krabbe, J. / Groll, M. / Hertweck, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.1 KB | Display | ![]() |
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PDB format | ![]() | 58.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.9 KB | Display | ![]() |
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Full document | ![]() | 437.3 KB | Display | |
Data in XML | ![]() | 8.9 KB | Display | |
Data in CIF | ![]() | 11.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7zhdSC S: Starting model for refinement C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 17550.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: Ccel_3263 / Plasmid: pET28a / Production host: ![]() ![]() | ||||
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#2: Chemical | ChemComp-GOL / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 2.8 M NaAc |
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-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 29, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 20682 / % possible obs: 99 % / Redundancy: 4.2 % / Rmerge(I) obs: 0.049 / Net I/σ(I): 16.4 |
Reflection shell | Resolution: 2→2.1 Å / Rmerge(I) obs: 0.582 / Mean I/σ(I) obs: 2.2 / Num. unique obs: 2807 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 7ZHD Resolution: 2→30 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.959 / SU B: 7.547 / SU ML: 0.088 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.147 / ESU R Free: 0.109 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 114.44 Å2 / Biso mean: 45.487 Å2 / Biso min: 29.22 Å2
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Refinement step | Cycle: final / Resolution: 2→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.052 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Origin x: -6.1331 Å / Origin y: -18.1165 Å / Origin z: -38.6975 Å
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