+
Open data
-
Basic information
Entry | Database: PDB / ID: 6pbs | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Structure of ClpC1-NTD in complex with Ecumicin | ||||||||||||
![]() |
| ||||||||||||
![]() | CHAPERONE/ANTIBIOTIC / ClpC1-NTD / Ecumicin / ATPase / Mycobacterium tuberculosis / CHAPERONE-ANTIBIOTIC complex | ||||||||||||
Function / homology | ![]() protein folding chaperone / peptidoglycan-based cell wall / cellular response to heat / protein homodimerization activity / ATP hydrolysis activity / ATP binding / plasma membrane / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Abad-Zapatero, C. / Wolf, N.M. | ||||||||||||
![]() | ![]() Title: Structure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions. Authors: Wolf, N.M. / Lee, H. / Zagal, D. / Nam, J.W. / Oh, D.C. / Lee, H. / Suh, J.W. / Pauli, G.F. / Cho, S. / Abad-Zapatero, C. | ||||||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 425.6 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 359.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 707.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 789.9 KB | Display | |
Data in XML | ![]() | 85.2 KB | Display | |
Data in CIF | ![]() | 115.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6pbaSC ![]() 6pbqC ![]() 6ucrC S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
-
Components
#1: Protein | Mass: 17529.131 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | #3: Chemical | ChemComp-ACT / #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.82 % |
---|---|
Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.2 M calcium acetate hydrate, 0.1 M Tris, pH 7.0, 20% PEG3000 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 23, 2017 |
Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→40 Å / Num. obs: 79421 / % possible obs: 98.8 % / Redundancy: 4.9 % / Rmerge(I) obs: 0.075 / Rpim(I) all: 0.041 / Rrim(I) all: 0.098 / Net I/σ(I): 21.5 |
Reflection shell | Resolution: 2.5→2.54 Å / Rmerge(I) obs: 0.638 / Num. unique obs: 3828 / Rpim(I) all: 0.364 / Rrim(I) all: 0.786 |
-
Processing
Software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: 6pba Resolution: 2.5→40 Å / Cross valid method: FREE R-VALUE Stereochemistry target values: GEOSTD + MONOMER LIBRARY + CDL V1.2
| ||||||||||||||||
Displacement parameters | Biso mean: 64.05 Å2 | ||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→40 Å
|