+Open data
-Basic information
Entry | Database: PDB / ID: 1hx5 | ||||||
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Title | Crystal structure of M. tuberculosis chaperonin-10 | ||||||
Components | 10 KDA CHAPERONIN | ||||||
Keywords | CHAPERONE / beta barrel / mobile loop / Structural Genomics / PSI / Protein Structure Initiative / TB Structural Genomics Consortium / TBSGC | ||||||
Function / homology | Function and homology information zymogen binding / cell wall / chaperone cofactor-dependent protein refolding / protein folding chaperone / peptidoglycan-based cell wall / unfolded protein binding / cellular response to heat / response to heat / protein-folding chaperone binding / 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 / response to heat / protein-folding chaperone binding / 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 | Mycobacterium tuberculosis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | ||||||
Authors | Taneja, B. / Mande, S.C. / TB Structural Genomics Consortium (TBSGC) | ||||||
Citation | 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: Journal: To be Published 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hx5.cif.gz | 103.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hx5.ent.gz | 85.2 KB | Display | PDB format |
PDBx/mmJSON format | 1hx5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hx/1hx5 ftp://data.pdbj.org/pub/pdb/validation_reports/hx/1hx5 | HTTPS FTP |
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-Related structure data
Related structure data | 1lepS S: Starting model for refinement |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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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.) Mycobacterium tuberculosis (bacteria) / Gene: RV3418C / Plasmid: PMAL-C / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P09621, UniProt: P9WPE5*PLUS |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
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 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT 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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