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Open data
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Basic information
Entry | Database: PDB / ID: 1hx5 | ||||||
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Title | Crystal structure of M. tuberculosis chaperonin-10 | ||||||
![]() | 10 KDA CHAPERONIN | ||||||
![]() | CHAPERONE / beta barrel / mobile loop / Structural Genomics / PSI / Protein Structure Initiative / TB Structural Genomics Consortium / TBSGC | ||||||
Function / homology | ![]() zymogen binding / cell wall / chaperone cofactor-dependent protein refolding / protein folding chaperone / peptidoglycan-based cell wall / unfolded protein binding / cellular response to heat / protein-folding chaperone binding / response to heat / response to antibiotic ...zymogen binding / cell wall / chaperone cofactor-dependent protein refolding / protein folding chaperone / peptidoglycan-based cell wall / unfolded protein binding / cellular response to heat / protein-folding chaperone binding / response to heat / response to antibiotic / regulation of DNA-templated transcription / ATP hydrolysis activity / extracellular region / ATP binding / metal ion binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Taneja, B. / Mande, S.C. / TB Structural Genomics Consortium (TBSGC) | ||||||
![]() | Journal: CURR.SCI. / Year: 2001 Title: Three-dimensional Structure of Mycobacterium tuberculosis Chaperonin-10 Reveals a Partially Stable Conformation for its Mobile Loop Authors: Taneja, B. / Mande, S.C. #1: ![]() Title: Crystal Structure of Mycobacterium tuberculosis Chaperonin-10 at 3.5 ang Resolution Authors: Taneja, B. / Mande, S.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 | ![]() | 103.9 KB | Display | ![]() |
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PDB format | ![]() | 85.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 469.1 KB | Display | ![]() |
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Full document | ![]() | 492.2 KB | Display | |
Data in XML | ![]() | 23 KB | Display | |
Data in CIF | ![]() | 32.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1lepS S: Starting model for refinement |
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Similar structure data | |
Other databases |
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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: 10684.979 Da / Num. of mol.: 7 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.64 Å3/Da / Density % sol: 53.47 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4 Details: PEG 400, lithium sulphate, sodium acetate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 15, 2000 / Details: mirrors |
Radiation | Monochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→30 Å / Num. all: 9954 / Num. obs: 9927 / % possible obs: 96.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.7 % / Biso Wilson estimate: 68.6 Å2 / Rmerge(I) obs: 0.078 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 3.5→3.77 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.28 / % possible all: 90.5 |
Reflection | *PLUS Lowest resolution: 30 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1LEP Resolution: 3.5→30 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh and Huber
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Refinement step | Cycle: LAST / Resolution: 3.5→30 Å
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Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 30 Å / σ(F): 0 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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