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The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation I in the presence of DnaK chaperone and a model substrate
- Authors
- Yin, YantingLi, Huilin
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data used to describe the Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation I in the presence of DnaK chaperone and a model substrate. The main summary display for this entry includes information on the experimental method, validation, macromolecules,...
- Subject
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Endopeptidase ClpMolecular Chaperones
- Access Rights
- Free to All
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The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined N-terminal domain in the presence of DnaK chaperone and a model substrate
- Authors
- Yin, YantingLi, Huilin
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data used to describe the Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined N-terminal domain in the presence of DnaK chaperone and a model substrate. The main summary display for this entry includes information on the experimental method,...
- Subject
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Endopeptidase ClpMolecular Chaperones
- Access Rights
- Free to All
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The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with three locally refined ClpB middle domains and three DnaK nucleotide binding domains
- Authors
- Yin, YantingLi, Huilin
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data used to describe the Mycobacterium tuberculosis ClpB disaggregase hexamer structure with three locally refined ClpB middle domains and three DnaK nucleotide binding domains The main summary display for this entry includes information on the experimental method, validation,...
- Subject
-
Endopeptidase ClpMolecular Chaperones
- Access Rights
- Free to All
-
The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined ClpB middle domain and a DnaK nucleotide binding domain
- Authors
- Yin, YantingLi, Huilin
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes cryogenic electron microscopy data used to describe the Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined ClpB middle domain and a DnaK nucleotide binding domain. The main summary display for this entry includes information on the experimental method, validation,...
- Subject
-
Endopeptidase ClpMolecular Chaperones
- Access Rights
- Free to All
-
The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation II in the presence of DnaK chaperone and a model substrate
- Authors
- Yin, YantingLi, Huilin
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data used to describe the Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation II in the presence of DnaK chaperone and a model substrate. The main summary display for this entry includes information on the experimental method, validation, macromolecules,...
- Subject
-
Endopeptidase ClpMolecular Chaperones
- Access Rights
- Free to All
-
The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation T in the presence of DnaK chaperone and a model substrate
- Authors
- Yin, YantingLi, Huilin
- Description
This deposit in the Research Collaboratory for Structural Bioinformatics Protein Data Base (PDB) includes electron microscopy data used to describe the Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation T in the presence of DnaK chaperone and a model substrate. The main summary display for this entry includes information on the experimental method, validation, macromolecules,...
- Subject
-
Endopeptidase ClpMolecular Chaperones
- Access Rights
- Free to All